r centenaria  (ATCC)


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    ATCC r centenaria
    Domain structure of the Ppr photosensor protein of R. <t>centenaria</t> . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.
    R Centenaria, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway"

    Article Title: The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway

    Journal: BMC Microbiology

    doi: 10.1186/1471-2180-10-281

    Domain structure of the Ppr photosensor protein of R. centenaria . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.
    Figure Legend Snippet: Domain structure of the Ppr photosensor protein of R. centenaria . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.

    Techniques Used: Binding Assay, Mutagenesis

    Interaction between Pph and the chemotactic protein Rc-CheW. (A) The binding of the histidine kinase domain Pph and CheW was analyzed in pull-down assays. R. centenaria 6his-Rc-CheW was expressed in E. coli C41 cells and purified. The Pph protein was translated in vitro in the presence of [ 35 S]-methionine (lane 1 and 4). Rc-CheW was added (50 μg) to the reaction and incubated at 37°C. The sample was applied to a Cu-Sepharose column and after washing the bound complexes were eluted (lanes 3 and 6). The fractions were analysed by phosphorimaging. The in vitro translating protein extracts are shown in lanes 1 and 4, the final wash steps in lanes 2 and 5 and the elution fractions in lanes 3 and 6, respectively. The co-elution rate was calculated and is indicated. The positions of molecular weight markers are indicated. (B) The binding of the Pph protein and Rc-CheW was analysed in the presence of ATP. The Pph protein was translated and Rc-CheW was added as described in (A). ATP or apyrase was added to each reaction as indicated and the samples were analysed as described in (A). The co-elution rate was calculated and is indicated in % as bound Pph protein.
    Figure Legend Snippet: Interaction between Pph and the chemotactic protein Rc-CheW. (A) The binding of the histidine kinase domain Pph and CheW was analyzed in pull-down assays. R. centenaria 6his-Rc-CheW was expressed in E. coli C41 cells and purified. The Pph protein was translated in vitro in the presence of [ 35 S]-methionine (lane 1 and 4). Rc-CheW was added (50 μg) to the reaction and incubated at 37°C. The sample was applied to a Cu-Sepharose column and after washing the bound complexes were eluted (lanes 3 and 6). The fractions were analysed by phosphorimaging. The in vitro translating protein extracts are shown in lanes 1 and 4, the final wash steps in lanes 2 and 5 and the elution fractions in lanes 3 and 6, respectively. The co-elution rate was calculated and is indicated. The positions of molecular weight markers are indicated. (B) The binding of the Pph protein and Rc-CheW was analysed in the presence of ATP. The Pph protein was translated and Rc-CheW was added as described in (A). ATP or apyrase was added to each reaction as indicated and the samples were analysed as described in (A). The co-elution rate was calculated and is indicated in % as bound Pph protein.

    Techniques Used: Binding Assay, Purification, In Vitro, Incubation, Co-Elution Assay, Molecular Weight

    Oligomeric state of the histidine kinase Pph. (A) Alignment of the dimerization domains of the Pph protein from R. centenaria and EnvZ from E. coli . The identity was 27% whereas the similarity was calculated with about 57%. The alignment was performed with the Clustal X software. (B) Purified Pph was analysed by gel filtration on a Sephadex G-200 column. Aliquots of the elution fractions (39-48) were separated by SDS-PAGE and blotted on a nitrocellulose membrane. The Pph protein was detected with a conjugate raised against the C-terminal StrepTag II. The position of the Pph protein is indicated. The following proteins werde used as molecular weight markers: β-amylase (200 kDa), alcohol dehydrogenase (150 kDa), albumin (66 kDa), carboanhydrase (29 kDa) and cytochrome c (12 kDa) were used.
    Figure Legend Snippet: Oligomeric state of the histidine kinase Pph. (A) Alignment of the dimerization domains of the Pph protein from R. centenaria and EnvZ from E. coli . The identity was 27% whereas the similarity was calculated with about 57%. The alignment was performed with the Clustal X software. (B) Purified Pph was analysed by gel filtration on a Sephadex G-200 column. Aliquots of the elution fractions (39-48) were separated by SDS-PAGE and blotted on a nitrocellulose membrane. The Pph protein was detected with a conjugate raised against the C-terminal StrepTag II. The position of the Pph protein is indicated. The following proteins werde used as molecular weight markers: β-amylase (200 kDa), alcohol dehydrogenase (150 kDa), albumin (66 kDa), carboanhydrase (29 kDa) and cytochrome c (12 kDa) were used.

    Techniques Used: Software, Purification, Filtration, SDS Page, Molecular Weight

    Protein complexes containing Pph isolated from R. centenaria . The Pph protein C-terminally fused to a strep-tag was expressed in R. centenaria and bound to a streptactin-Sepharose column. The elution fractions were analyzed by SDS-PAGE, silver staining (A) and Western blot with antibodies to strep-tag II (B) or to Rc-CheW (C), respectively. The crude protein extract (lanes 1 and 4), the last washing step (lanes 2 and 5) as well as the elution step (lanes 3 and 6) are shown. The positions of molecular weight markers are indicated.
    Figure Legend Snippet: Protein complexes containing Pph isolated from R. centenaria . The Pph protein C-terminally fused to a strep-tag was expressed in R. centenaria and bound to a streptactin-Sepharose column. The elution fractions were analyzed by SDS-PAGE, silver staining (A) and Western blot with antibodies to strep-tag II (B) or to Rc-CheW (C), respectively. The crude protein extract (lanes 1 and 4), the last washing step (lanes 2 and 5) as well as the elution step (lanes 3 and 6) are shown. The positions of molecular weight markers are indicated.

    Techniques Used: Isolation, Strep-tag, SDS Page, Silver Staining, Western Blot, Molecular Weight

    r centenaria  (ATCC)


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    ATCC r centenaria
    Domain structure of the Ppr photosensor protein of R. <t>centenaria</t> . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.
    R Centenaria, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway"

    Article Title: The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway

    Journal: BMC Microbiology

    doi: 10.1186/1471-2180-10-281

    Domain structure of the Ppr photosensor protein of R. centenaria . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.
    Figure Legend Snippet: Domain structure of the Ppr photosensor protein of R. centenaria . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.

    Techniques Used: Binding Assay, Mutagenesis

    Interaction between Pph and the chemotactic protein Rc-CheW. (A) The binding of the histidine kinase domain Pph and CheW was analyzed in pull-down assays. R. centenaria 6his-Rc-CheW was expressed in E. coli C41 cells and purified. The Pph protein was translated in vitro in the presence of [ 35 S]-methionine (lane 1 and 4). Rc-CheW was added (50 μg) to the reaction and incubated at 37°C. The sample was applied to a Cu-Sepharose column and after washing the bound complexes were eluted (lanes 3 and 6). The fractions were analysed by phosphorimaging. The in vitro translating protein extracts are shown in lanes 1 and 4, the final wash steps in lanes 2 and 5 and the elution fractions in lanes 3 and 6, respectively. The co-elution rate was calculated and is indicated. The positions of molecular weight markers are indicated. (B) The binding of the Pph protein and Rc-CheW was analysed in the presence of ATP. The Pph protein was translated and Rc-CheW was added as described in (A). ATP or apyrase was added to each reaction as indicated and the samples were analysed as described in (A). The co-elution rate was calculated and is indicated in % as bound Pph protein.
    Figure Legend Snippet: Interaction between Pph and the chemotactic protein Rc-CheW. (A) The binding of the histidine kinase domain Pph and CheW was analyzed in pull-down assays. R. centenaria 6his-Rc-CheW was expressed in E. coli C41 cells and purified. The Pph protein was translated in vitro in the presence of [ 35 S]-methionine (lane 1 and 4). Rc-CheW was added (50 μg) to the reaction and incubated at 37°C. The sample was applied to a Cu-Sepharose column and after washing the bound complexes were eluted (lanes 3 and 6). The fractions were analysed by phosphorimaging. The in vitro translating protein extracts are shown in lanes 1 and 4, the final wash steps in lanes 2 and 5 and the elution fractions in lanes 3 and 6, respectively. The co-elution rate was calculated and is indicated. The positions of molecular weight markers are indicated. (B) The binding of the Pph protein and Rc-CheW was analysed in the presence of ATP. The Pph protein was translated and Rc-CheW was added as described in (A). ATP or apyrase was added to each reaction as indicated and the samples were analysed as described in (A). The co-elution rate was calculated and is indicated in % as bound Pph protein.

    Techniques Used: Binding Assay, Purification, In Vitro, Incubation, Co-Elution Assay, Molecular Weight

    Oligomeric state of the histidine kinase Pph. (A) Alignment of the dimerization domains of the Pph protein from R. centenaria and EnvZ from E. coli . The identity was 27% whereas the similarity was calculated with about 57%. The alignment was performed with the Clustal X software. (B) Purified Pph was analysed by gel filtration on a Sephadex G-200 column. Aliquots of the elution fractions (39-48) were separated by SDS-PAGE and blotted on a nitrocellulose membrane. The Pph protein was detected with a conjugate raised against the C-terminal StrepTag II. The position of the Pph protein is indicated. The following proteins werde used as molecular weight markers: β-amylase (200 kDa), alcohol dehydrogenase (150 kDa), albumin (66 kDa), carboanhydrase (29 kDa) and cytochrome c (12 kDa) were used.
    Figure Legend Snippet: Oligomeric state of the histidine kinase Pph. (A) Alignment of the dimerization domains of the Pph protein from R. centenaria and EnvZ from E. coli . The identity was 27% whereas the similarity was calculated with about 57%. The alignment was performed with the Clustal X software. (B) Purified Pph was analysed by gel filtration on a Sephadex G-200 column. Aliquots of the elution fractions (39-48) were separated by SDS-PAGE and blotted on a nitrocellulose membrane. The Pph protein was detected with a conjugate raised against the C-terminal StrepTag II. The position of the Pph protein is indicated. The following proteins werde used as molecular weight markers: β-amylase (200 kDa), alcohol dehydrogenase (150 kDa), albumin (66 kDa), carboanhydrase (29 kDa) and cytochrome c (12 kDa) were used.

    Techniques Used: Software, Purification, Filtration, SDS Page, Molecular Weight

    Protein complexes containing Pph isolated from R. centenaria . The Pph protein C-terminally fused to a strep-tag was expressed in R. centenaria and bound to a streptactin-Sepharose column. The elution fractions were analyzed by SDS-PAGE, silver staining (A) and Western blot with antibodies to strep-tag II (B) or to Rc-CheW (C), respectively. The crude protein extract (lanes 1 and 4), the last washing step (lanes 2 and 5) as well as the elution step (lanes 3 and 6) are shown. The positions of molecular weight markers are indicated.
    Figure Legend Snippet: Protein complexes containing Pph isolated from R. centenaria . The Pph protein C-terminally fused to a strep-tag was expressed in R. centenaria and bound to a streptactin-Sepharose column. The elution fractions were analyzed by SDS-PAGE, silver staining (A) and Western blot with antibodies to strep-tag II (B) or to Rc-CheW (C), respectively. The crude protein extract (lanes 1 and 4), the last washing step (lanes 2 and 5) as well as the elution step (lanes 3 and 6) are shown. The positions of molecular weight markers are indicated.

    Techniques Used: Isolation, Strep-tag, SDS Page, Silver Staining, Western Blot, Molecular Weight

    rhodospirillium centenum atcc 43720  (ATCC)


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    ATCC rhodospirillium centenum atcc 43720
    Rhodospirillium Centenum Atcc 43720, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    centenum strain atcc 43720  (ATCC)


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    ATCC centenum strain atcc 43720
    Centenum Strain Atcc 43720, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    azospirillum halopraeferens au4t x79731 rhodocista centenaria atcc 43720t  (ATCC)


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    ATCC azospirillum halopraeferens au4t x79731 rhodocista centenaria atcc 43720t
    Azospirillum Halopraeferens Au4t X79731 Rhodocista Centenaria Atcc 43720t, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    centenum  (ATCC)


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    ATCC centenum
    Sequence alignment of the predicted CrtJ proteins <t>of</t> <t>Rsp.</t> <t>centenum</t> to homologous proteins in other purple bacteria. Abbreviations and their meaning: Rcen; Rsp. centenum, Rcap; Rba. capsulatus, Rsph; Rba. sphaeroides, Rgel; Rbv. gelatinosus. Accession numbers of the sequences are AB369262, P26167, ABA79455 and BAA94062, respectively.
    Centenum, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Regulation of aerobic photosystem synthesis in the purple bacterium Rhodospirillum centenum by CrtJ and AerR"

    Article Title: Regulation of aerobic photosystem synthesis in the purple bacterium Rhodospirillum centenum by CrtJ and AerR

    Journal:

    doi: 10.1039/b802365b

    Sequence alignment of the predicted CrtJ proteins of Rsp. centenum to homologous proteins in other purple bacteria. Abbreviations and their meaning: Rcen; Rsp. centenum, Rcap; Rba. capsulatus, Rsph; Rba. sphaeroides, Rgel; Rbv. gelatinosus. Accession numbers of the sequences are AB369262, P26167, ABA79455 and BAA94062, respectively.
    Figure Legend Snippet: Sequence alignment of the predicted CrtJ proteins of Rsp. centenum to homologous proteins in other purple bacteria. Abbreviations and their meaning: Rcen; Rsp. centenum, Rcap; Rba. capsulatus, Rsph; Rba. sphaeroides, Rgel; Rbv. gelatinosus. Accession numbers of the sequences are AB369262, P26167, ABA79455 and BAA94062, respectively.

    Techniques Used: Sequencing

    Absorption spectra of Rsp. centenum wild type (solid lines), AERR1 (short dashed lines) and CRTJ1 (long dashed line) grown anaerobically (panel A) or aerobically (panel B). AERR1 is the aerR-disrupted strain, and CRTJ1 is the crtJ-disrupted strain. The spectrum for CRTJ1 cells grown anaerobically is not shown, but identical to that of the wild type cells (panel A, solid line).
    Figure Legend Snippet: Absorption spectra of Rsp. centenum wild type (solid lines), AERR1 (short dashed lines) and CRTJ1 (long dashed line) grown anaerobically (panel A) or aerobically (panel B). AERR1 is the aerR-disrupted strain, and CRTJ1 is the crtJ-disrupted strain. The spectrum for CRTJ1 cells grown anaerobically is not shown, but identical to that of the wild type cells (panel A, solid line).

    Techniques Used:

    Comparison of possible promoter sequences found in Rsp. centenum crtE and crtD genes and those reported in Rba. capsulatus photosynthesis genes. The number in parentheses indicates the number of nucleotides between the start codon, ATG, and the right end of the sequence. The proposed CrtJ-binding sites (TGT-N12-ACA) are shown in bold. Nucleotide sequences of the consensus E. coli σ70 recognition site are shown in the bottom.
    Figure Legend Snippet: Comparison of possible promoter sequences found in Rsp. centenum crtE and crtD genes and those reported in Rba. capsulatus photosynthesis genes. The number in parentheses indicates the number of nucleotides between the start codon, ATG, and the right end of the sequence. The proposed CrtJ-binding sites (TGT-N12-ACA) are shown in bold. Nucleotide sequences of the consensus E. coli σ70 recognition site are shown in the bottom.

    Techniques Used: Sequencing, Binding Assay

    Comparison of readthrough transcription for puf operon between Rba. capsulatus and Rsp. centenum. Thickness of the arrows indicates the levels of transcription. The dotted lines donate possible gene locations and transcripts that have not been experimentally proven. Asterisks denote the major transcripts for puf operon.
    Figure Legend Snippet: Comparison of readthrough transcription for puf operon between Rba. capsulatus and Rsp. centenum. Thickness of the arrows indicates the levels of transcription. The dotted lines donate possible gene locations and transcripts that have not been experimentally proven. Asterisks denote the major transcripts for puf operon.

    Techniques Used:

    centenum  (ATCC)


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    ATCC centenum
    Sequence alignment of the predicted CrtJ proteins <t>of</t> <t>Rsp.</t> <t>centenum</t> to homologous proteins in other purple bacteria. Abbreviations and their meaning: Rcen; Rsp. centenum, Rcap; Rba. capsulatus, Rsph; Rba. sphaeroides, Rgel; Rbv. gelatinosus. Accession numbers of the sequences are AB369262, P26167, ABA79455 and BAA94062, respectively.
    Centenum, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Regulation of aerobic photosystem synthesis in the purple bacterium Rhodospirillum centenum by CrtJ and AerR "

    Article Title: Regulation of aerobic photosystem synthesis in the purple bacterium Rhodospirillum centenum by CrtJ and AerR

    Journal:

    doi: 10.1039/b802365b

    Sequence alignment of the predicted CrtJ proteins of Rsp. centenum to homologous proteins in other purple bacteria. Abbreviations and their meaning: Rcen; Rsp. centenum, Rcap; Rba. capsulatus, Rsph; Rba. sphaeroides, Rgel; Rbv. gelatinosus. Accession numbers of the sequences are AB369262, P26167, ABA79455 and BAA94062, respectively.
    Figure Legend Snippet: Sequence alignment of the predicted CrtJ proteins of Rsp. centenum to homologous proteins in other purple bacteria. Abbreviations and their meaning: Rcen; Rsp. centenum, Rcap; Rba. capsulatus, Rsph; Rba. sphaeroides, Rgel; Rbv. gelatinosus. Accession numbers of the sequences are AB369262, P26167, ABA79455 and BAA94062, respectively.

    Techniques Used: Sequencing

    Absorption spectra of Rsp. centenum wild type (solid lines), AERR1 (short dashed lines) and CRTJ1 (long dashed line) grown anaerobically (panel A) or aerobically (panel B). AERR1 is the aerR-disrupted strain, and CRTJ1 is the crtJ-disrupted strain. The spectrum for CRTJ1 cells grown anaerobically is not shown, but identical to that of the wild type cells (panel A, solid line).
    Figure Legend Snippet: Absorption spectra of Rsp. centenum wild type (solid lines), AERR1 (short dashed lines) and CRTJ1 (long dashed line) grown anaerobically (panel A) or aerobically (panel B). AERR1 is the aerR-disrupted strain, and CRTJ1 is the crtJ-disrupted strain. The spectrum for CRTJ1 cells grown anaerobically is not shown, but identical to that of the wild type cells (panel A, solid line).

    Techniques Used:

    Comparison of possible promoter sequences found in Rsp. centenum crtE and crtD genes and those reported in Rba. capsulatus photosynthesis genes. The number in parentheses indicates the number of nucleotides between the start codon, ATG, and the right end of the sequence. The proposed CrtJ-binding sites (TGT-N12-ACA) are shown in bold. Nucleotide sequences of the consensus E. coli σ70 recognition site are shown in the bottom.
    Figure Legend Snippet: Comparison of possible promoter sequences found in Rsp. centenum crtE and crtD genes and those reported in Rba. capsulatus photosynthesis genes. The number in parentheses indicates the number of nucleotides between the start codon, ATG, and the right end of the sequence. The proposed CrtJ-binding sites (TGT-N12-ACA) are shown in bold. Nucleotide sequences of the consensus E. coli σ70 recognition site are shown in the bottom.

    Techniques Used: Sequencing, Binding Assay

    Comparison of readthrough transcription for puf operon between Rba. capsulatus and Rsp. centenum. Thickness of the arrows indicates the levels of transcription. The dotted lines donate possible gene locations and transcripts that have not been experimentally proven. Asterisks denote the major transcripts for puf operon.
    Figure Legend Snippet: Comparison of readthrough transcription for puf operon between Rba. capsulatus and Rsp. centenum. Thickness of the arrows indicates the levels of transcription. The dotted lines donate possible gene locations and transcripts that have not been experimentally proven. Asterisks denote the major transcripts for puf operon.

    Techniques Used:

    rhodocista centenaria atcc 43720t  (ATCC)


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    ATCC rhodocista centenaria atcc 43720t
    Rhodocista Centenaria Atcc 43720t, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rhodocista centenaria atcc 43720t  (ATCC)


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    ATCC rhodocista centenaria atcc 43720t
    Rhodocista Centenaria Atcc 43720t, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rhodocista centenaria atcc 43720t  (ATCC)


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    ATCC rhodocista centenaria atcc 43720t
    Rhodocista Centenaria Atcc 43720t, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    43720t  (ATCC)


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    ATCC 43720t
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    ATCC r centenaria
    Domain structure of the Ppr photosensor protein of R. <t>centenaria</t> . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.
    R Centenaria, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    ATCC rhodospirillium centenum atcc 43720
    Domain structure of the Ppr photosensor protein of R. <t>centenaria</t> . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.
    Rhodospirillium Centenum Atcc 43720, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    ATCC centenum strain atcc 43720
    Domain structure of the Ppr photosensor protein of R. <t>centenaria</t> . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.
    Centenum Strain Atcc 43720, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    ATCC azospirillum halopraeferens au4t x79731 rhodocista centenaria atcc 43720t
    Domain structure of the Ppr photosensor protein of R. <t>centenaria</t> . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.
    Azospirillum Halopraeferens Au4t X79731 Rhodocista Centenaria Atcc 43720t, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    ATCC centenum
    Sequence alignment of the predicted CrtJ proteins <t>of</t> <t>Rsp.</t> <t>centenum</t> to homologous proteins in other purple bacteria. Abbreviations and their meaning: Rcen; Rsp. centenum, Rcap; Rba. capsulatus, Rsph; Rba. sphaeroides, Rgel; Rbv. gelatinosus. Accession numbers of the sequences are AB369262, P26167, ABA79455 and BAA94062, respectively.
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    ATCC rhodocista centenaria atcc 43720t
    Sequence alignment of the predicted CrtJ proteins <t>of</t> <t>Rsp.</t> <t>centenum</t> to homologous proteins in other purple bacteria. Abbreviations and their meaning: Rcen; Rsp. centenum, Rcap; Rba. capsulatus, Rsph; Rba. sphaeroides, Rgel; Rbv. gelatinosus. Accession numbers of the sequences are AB369262, P26167, ABA79455 and BAA94062, respectively.
    Rhodocista Centenaria Atcc 43720t, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    43720t  (ATCC)
    92
    ATCC 43720t
    Sequence alignment of the predicted CrtJ proteins <t>of</t> <t>Rsp.</t> <t>centenum</t> to homologous proteins in other purple bacteria. Abbreviations and their meaning: Rcen; Rsp. centenum, Rcap; Rba. capsulatus, Rsph; Rba. sphaeroides, Rgel; Rbv. gelatinosus. Accession numbers of the sequences are AB369262, P26167, ABA79455 and BAA94062, respectively.
    43720t, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Domain structure of the Ppr photosensor protein of R. centenaria . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.

    Journal: BMC Microbiology

    Article Title: The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway

    doi: 10.1186/1471-2180-10-281

    Figure Lengend Snippet: Domain structure of the Ppr photosensor protein of R. centenaria . The Ppr protein consists of a photoactive yellow protein domain (Pyp; residues 1-135) which carries the blue light absorbing chromophore p -hydroxycinnamic acid, a central bacteriophytochrome bilin binding domain (residues 136-601) with the red light absorbing biliverdin chromophore, and a histidine kinase domain (Pph; residues 602-884). The truncated Pph protein consists of the histidine kinase domain (residues 602-884). In the mutant Pph H670A the putative autophosphorylated histidine residue (H670) is replaced by an alanine.

    Article Snippet: R. centenaria (ATCC 43720) was obtained from the culture collection. (For anaerobic photosynthetic growth R. centenaria was cultured in screw cap bottles filled to the top with PYVS medium [ ] and illuminated by an 80 W tungsten bulb (Concentra, Osram, Germany) at 42°C.

    Techniques: Binding Assay, Mutagenesis

    Interaction between Pph and the chemotactic protein Rc-CheW. (A) The binding of the histidine kinase domain Pph and CheW was analyzed in pull-down assays. R. centenaria 6his-Rc-CheW was expressed in E. coli C41 cells and purified. The Pph protein was translated in vitro in the presence of [ 35 S]-methionine (lane 1 and 4). Rc-CheW was added (50 μg) to the reaction and incubated at 37°C. The sample was applied to a Cu-Sepharose column and after washing the bound complexes were eluted (lanes 3 and 6). The fractions were analysed by phosphorimaging. The in vitro translating protein extracts are shown in lanes 1 and 4, the final wash steps in lanes 2 and 5 and the elution fractions in lanes 3 and 6, respectively. The co-elution rate was calculated and is indicated. The positions of molecular weight markers are indicated. (B) The binding of the Pph protein and Rc-CheW was analysed in the presence of ATP. The Pph protein was translated and Rc-CheW was added as described in (A). ATP or apyrase was added to each reaction as indicated and the samples were analysed as described in (A). The co-elution rate was calculated and is indicated in % as bound Pph protein.

    Journal: BMC Microbiology

    Article Title: The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway

    doi: 10.1186/1471-2180-10-281

    Figure Lengend Snippet: Interaction between Pph and the chemotactic protein Rc-CheW. (A) The binding of the histidine kinase domain Pph and CheW was analyzed in pull-down assays. R. centenaria 6his-Rc-CheW was expressed in E. coli C41 cells and purified. The Pph protein was translated in vitro in the presence of [ 35 S]-methionine (lane 1 and 4). Rc-CheW was added (50 μg) to the reaction and incubated at 37°C. The sample was applied to a Cu-Sepharose column and after washing the bound complexes were eluted (lanes 3 and 6). The fractions were analysed by phosphorimaging. The in vitro translating protein extracts are shown in lanes 1 and 4, the final wash steps in lanes 2 and 5 and the elution fractions in lanes 3 and 6, respectively. The co-elution rate was calculated and is indicated. The positions of molecular weight markers are indicated. (B) The binding of the Pph protein and Rc-CheW was analysed in the presence of ATP. The Pph protein was translated and Rc-CheW was added as described in (A). ATP or apyrase was added to each reaction as indicated and the samples were analysed as described in (A). The co-elution rate was calculated and is indicated in % as bound Pph protein.

    Article Snippet: R. centenaria (ATCC 43720) was obtained from the culture collection. (For anaerobic photosynthetic growth R. centenaria was cultured in screw cap bottles filled to the top with PYVS medium [ ] and illuminated by an 80 W tungsten bulb (Concentra, Osram, Germany) at 42°C.

    Techniques: Binding Assay, Purification, In Vitro, Incubation, Co-Elution Assay, Molecular Weight

    Oligomeric state of the histidine kinase Pph. (A) Alignment of the dimerization domains of the Pph protein from R. centenaria and EnvZ from E. coli . The identity was 27% whereas the similarity was calculated with about 57%. The alignment was performed with the Clustal X software. (B) Purified Pph was analysed by gel filtration on a Sephadex G-200 column. Aliquots of the elution fractions (39-48) were separated by SDS-PAGE and blotted on a nitrocellulose membrane. The Pph protein was detected with a conjugate raised against the C-terminal StrepTag II. The position of the Pph protein is indicated. The following proteins werde used as molecular weight markers: β-amylase (200 kDa), alcohol dehydrogenase (150 kDa), albumin (66 kDa), carboanhydrase (29 kDa) and cytochrome c (12 kDa) were used.

    Journal: BMC Microbiology

    Article Title: The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway

    doi: 10.1186/1471-2180-10-281

    Figure Lengend Snippet: Oligomeric state of the histidine kinase Pph. (A) Alignment of the dimerization domains of the Pph protein from R. centenaria and EnvZ from E. coli . The identity was 27% whereas the similarity was calculated with about 57%. The alignment was performed with the Clustal X software. (B) Purified Pph was analysed by gel filtration on a Sephadex G-200 column. Aliquots of the elution fractions (39-48) were separated by SDS-PAGE and blotted on a nitrocellulose membrane. The Pph protein was detected with a conjugate raised against the C-terminal StrepTag II. The position of the Pph protein is indicated. The following proteins werde used as molecular weight markers: β-amylase (200 kDa), alcohol dehydrogenase (150 kDa), albumin (66 kDa), carboanhydrase (29 kDa) and cytochrome c (12 kDa) were used.

    Article Snippet: R. centenaria (ATCC 43720) was obtained from the culture collection. (For anaerobic photosynthetic growth R. centenaria was cultured in screw cap bottles filled to the top with PYVS medium [ ] and illuminated by an 80 W tungsten bulb (Concentra, Osram, Germany) at 42°C.

    Techniques: Software, Purification, Filtration, SDS Page, Molecular Weight

    Protein complexes containing Pph isolated from R. centenaria . The Pph protein C-terminally fused to a strep-tag was expressed in R. centenaria and bound to a streptactin-Sepharose column. The elution fractions were analyzed by SDS-PAGE, silver staining (A) and Western blot with antibodies to strep-tag II (B) or to Rc-CheW (C), respectively. The crude protein extract (lanes 1 and 4), the last washing step (lanes 2 and 5) as well as the elution step (lanes 3 and 6) are shown. The positions of molecular weight markers are indicated.

    Journal: BMC Microbiology

    Article Title: The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway

    doi: 10.1186/1471-2180-10-281

    Figure Lengend Snippet: Protein complexes containing Pph isolated from R. centenaria . The Pph protein C-terminally fused to a strep-tag was expressed in R. centenaria and bound to a streptactin-Sepharose column. The elution fractions were analyzed by SDS-PAGE, silver staining (A) and Western blot with antibodies to strep-tag II (B) or to Rc-CheW (C), respectively. The crude protein extract (lanes 1 and 4), the last washing step (lanes 2 and 5) as well as the elution step (lanes 3 and 6) are shown. The positions of molecular weight markers are indicated.

    Article Snippet: R. centenaria (ATCC 43720) was obtained from the culture collection. (For anaerobic photosynthetic growth R. centenaria was cultured in screw cap bottles filled to the top with PYVS medium [ ] and illuminated by an 80 W tungsten bulb (Concentra, Osram, Germany) at 42°C.

    Techniques: Isolation, Strep-tag, SDS Page, Silver Staining, Western Blot, Molecular Weight

    Sequence alignment of the predicted CrtJ proteins of Rsp. centenum to homologous proteins in other purple bacteria. Abbreviations and their meaning: Rcen; Rsp. centenum, Rcap; Rba. capsulatus, Rsph; Rba. sphaeroides, Rgel; Rbv. gelatinosus. Accession numbers of the sequences are AB369262, P26167, ABA79455 and BAA94062, respectively.

    Journal:

    Article Title: Regulation of aerobic photosystem synthesis in the purple bacterium Rhodospirillum centenum by CrtJ and AerR

    doi: 10.1039/b802365b

    Figure Lengend Snippet: Sequence alignment of the predicted CrtJ proteins of Rsp. centenum to homologous proteins in other purple bacteria. Abbreviations and their meaning: Rcen; Rsp. centenum, Rcap; Rba. capsulatus, Rsph; Rba. sphaeroides, Rgel; Rbv. gelatinosus. Accession numbers of the sequences are AB369262, P26167, ABA79455 and BAA94062, respectively.

    Article Snippet: Bacterial strains and growth conditions The wild-type strain of Rsp. centenum (ATCC 43720), the aerR -disrupted strain AERR1, and the crtJ -disrupted strain CRTJ1 were grown at 42 °C in CENS medium as described previously.

    Techniques: Sequencing

    Absorption spectra of Rsp. centenum wild type (solid lines), AERR1 (short dashed lines) and CRTJ1 (long dashed line) grown anaerobically (panel A) or aerobically (panel B). AERR1 is the aerR-disrupted strain, and CRTJ1 is the crtJ-disrupted strain. The spectrum for CRTJ1 cells grown anaerobically is not shown, but identical to that of the wild type cells (panel A, solid line).

    Journal:

    Article Title: Regulation of aerobic photosystem synthesis in the purple bacterium Rhodospirillum centenum by CrtJ and AerR

    doi: 10.1039/b802365b

    Figure Lengend Snippet: Absorption spectra of Rsp. centenum wild type (solid lines), AERR1 (short dashed lines) and CRTJ1 (long dashed line) grown anaerobically (panel A) or aerobically (panel B). AERR1 is the aerR-disrupted strain, and CRTJ1 is the crtJ-disrupted strain. The spectrum for CRTJ1 cells grown anaerobically is not shown, but identical to that of the wild type cells (panel A, solid line).

    Article Snippet: Bacterial strains and growth conditions The wild-type strain of Rsp. centenum (ATCC 43720), the aerR -disrupted strain AERR1, and the crtJ -disrupted strain CRTJ1 were grown at 42 °C in CENS medium as described previously.

    Techniques:

    Comparison of possible promoter sequences found in Rsp. centenum crtE and crtD genes and those reported in Rba. capsulatus photosynthesis genes. The number in parentheses indicates the number of nucleotides between the start codon, ATG, and the right end of the sequence. The proposed CrtJ-binding sites (TGT-N12-ACA) are shown in bold. Nucleotide sequences of the consensus E. coli σ70 recognition site are shown in the bottom.

    Journal:

    Article Title: Regulation of aerobic photosystem synthesis in the purple bacterium Rhodospirillum centenum by CrtJ and AerR

    doi: 10.1039/b802365b

    Figure Lengend Snippet: Comparison of possible promoter sequences found in Rsp. centenum crtE and crtD genes and those reported in Rba. capsulatus photosynthesis genes. The number in parentheses indicates the number of nucleotides between the start codon, ATG, and the right end of the sequence. The proposed CrtJ-binding sites (TGT-N12-ACA) are shown in bold. Nucleotide sequences of the consensus E. coli σ70 recognition site are shown in the bottom.

    Article Snippet: Bacterial strains and growth conditions The wild-type strain of Rsp. centenum (ATCC 43720), the aerR -disrupted strain AERR1, and the crtJ -disrupted strain CRTJ1 were grown at 42 °C in CENS medium as described previously.

    Techniques: Sequencing, Binding Assay

    Comparison of readthrough transcription for puf operon between Rba. capsulatus and Rsp. centenum. Thickness of the arrows indicates the levels of transcription. The dotted lines donate possible gene locations and transcripts that have not been experimentally proven. Asterisks denote the major transcripts for puf operon.

    Journal:

    Article Title: Regulation of aerobic photosystem synthesis in the purple bacterium Rhodospirillum centenum by CrtJ and AerR

    doi: 10.1039/b802365b

    Figure Lengend Snippet: Comparison of readthrough transcription for puf operon between Rba. capsulatus and Rsp. centenum. Thickness of the arrows indicates the levels of transcription. The dotted lines donate possible gene locations and transcripts that have not been experimentally proven. Asterisks denote the major transcripts for puf operon.

    Article Snippet: Bacterial strains and growth conditions The wild-type strain of Rsp. centenum (ATCC 43720), the aerR -disrupted strain AERR1, and the crtJ -disrupted strain CRTJ1 were grown at 42 °C in CENS medium as described previously.

    Techniques: