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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    Structured Review

    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 centenum strain sw  (ATCC)


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    ATCC r centenum strain sw
    R Centenum Strain Sw, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    r centenum  (ATCC)


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    ATCC r centenum
    R Centenum, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    r centenum  (ATCC)


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    ATCC r centenum
    Representative images of WT R. <t>centenum</t> cells grown on <t>vegetative</t> <t>CENS</t> and cyst-inducing CENS 8×N media. (A) Smooth colony morphology (left), microscopic analysis of cells in the smooth colony (middle), and flow cytometry quantification of the number of cysts in colonies grown in CENS medium (right). (B) Rugose/wrinkled colony morphology characteristic of biofilms with the corresponding microscopic and flow cytometry analyses of cysts when grown on CENS 8×N solid medium. SSC, side scatter; FSC, forward scatter.
    R Centenum, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "No Light, No Germination: Excitation of the Rhodospirillum centenum Photosynthetic Apparatus Is Necessary and Sufficient for Cyst Germination"

    Article Title: No Light, No Germination: Excitation of the Rhodospirillum centenum Photosynthetic Apparatus Is Necessary and Sufficient for Cyst Germination

    Journal: mBio

    doi: 10.1128/mBio.03619-20

    Representative images of WT R. centenum cells grown on vegetative CENS and cyst-inducing CENS 8×N media. (A) Smooth colony morphology (left), microscopic analysis of cells in the smooth colony (middle), and flow cytometry quantification of the number of cysts in colonies grown in CENS medium (right). (B) Rugose/wrinkled colony morphology characteristic of biofilms with the corresponding microscopic and flow cytometry analyses of cysts when grown on CENS 8×N solid medium. SSC, side scatter; FSC, forward scatter.
    Figure Legend Snippet: Representative images of WT R. centenum cells grown on vegetative CENS and cyst-inducing CENS 8×N media. (A) Smooth colony morphology (left), microscopic analysis of cells in the smooth colony (middle), and flow cytometry quantification of the number of cysts in colonies grown in CENS medium (right). (B) Rugose/wrinkled colony morphology characteristic of biofilms with the corresponding microscopic and flow cytometry analyses of cysts when grown on CENS 8×N solid medium. SSC, side scatter; FSC, forward scatter.

    Techniques Used: Flow Cytometry

    wild type r centenum atcc 51521  (ATCC)


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    ATCC wild type r centenum atcc 51521
    Wild Type R Centenum Atcc 51521, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    r centenum atcc 51521 genome  (ATCC)


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    ATCC r centenum atcc 51521 genome
    R Centenum Atcc 51521 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    base pair r centenum atcc 51521 genome  (ATCC)


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    ATCC base pair r centenum atcc 51521 genome
    Base Pair R Centenum Atcc 51521 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    base pair r centenum atcc 51521 genome  (ATCC)


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    ATCC base pair r centenum atcc 51521 genome
    Base Pair R Centenum Atcc 51521 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    type r centenum strain atcc 51521  (ATCC)


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    ATCC type r centenum strain atcc 51521
    Type R Centenum Strain Atcc 51521, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    r centenum strain  (ATCC)


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    ATCC r centenum strain
    R Centenum Strain, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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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    ATCC r centenum strain sw
    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 Centenum Strain Sw, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC r centenum
    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 Centenum, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC wild type r centenum atcc 51521
    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.
    Wild Type R Centenum Atcc 51521, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC r centenum atcc 51521 genome
    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 Centenum Atcc 51521 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 1 article reviews
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    93
    ATCC base pair r centenum atcc 51521 genome
    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.
    Base Pair R Centenum Atcc 51521 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    ATCC type r centenum strain atcc 51521
    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.
    Type R Centenum Strain Atcc 51521, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    ATCC r centenum strain
    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 Centenum Strain, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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