cariogenic strains streptococcus mutans  (ATCC)


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    ATCC cariogenic strains streptococcus mutans
    Anti-microbial activity of clinical working concentrations of PHMG-P (1%) and CHX (0.2%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. <t>mutans</t> and L. acidophilus ).
    Cariogenic Strains Streptococcus Mutans, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Antimicrobial activity of polyhexamethylene guanidine phosphate in comparison to chlorhexidine using the quantitative suspension method"

    Article Title: Antimicrobial activity of polyhexamethylene guanidine phosphate in comparison to chlorhexidine using the quantitative suspension method

    Journal: Annals of Clinical Microbiology and Antimicrobials

    doi: 10.1186/s12941-015-0097-x

    Anti-microbial activity of clinical working concentrations of PHMG-P (1%) and CHX (0.2%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).
    Figure Legend Snippet: Anti-microbial activity of clinical working concentrations of PHMG-P (1%) and CHX (0.2%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).

    Techniques Used: Activity Assay

    Anti-microbial activity of highly diluted PHMG-P (0.05%) and CHX (0.05%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).
    Figure Legend Snippet: Anti-microbial activity of highly diluted PHMG-P (0.05%) and CHX (0.05%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).

    Techniques Used: Activity Assay

    cariogenic strains streptococcus mutans  (ATCC)


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    ATCC cariogenic strains streptococcus mutans
    Anti-microbial activity of clinical working concentrations of PHMG-P (1%) and CHX (0.2%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. <t>mutans</t> and L. acidophilus ).
    Cariogenic Strains Streptococcus Mutans, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Antimicrobial activity of polyhexamethylene guanidine phosphate in comparison to chlorhexidine using the quantitative suspension method"

    Article Title: Antimicrobial activity of polyhexamethylene guanidine phosphate in comparison to chlorhexidine using the quantitative suspension method

    Journal: Annals of Clinical Microbiology and Antimicrobials

    doi: 10.1186/s12941-015-0097-x

    Anti-microbial activity of clinical working concentrations of PHMG-P (1%) and CHX (0.2%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).
    Figure Legend Snippet: Anti-microbial activity of clinical working concentrations of PHMG-P (1%) and CHX (0.2%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).

    Techniques Used: Activity Assay

    Anti-microbial activity of highly diluted PHMG-P (0.05%) and CHX (0.05%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).
    Figure Legend Snippet: Anti-microbial activity of highly diluted PHMG-P (0.05%) and CHX (0.05%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).

    Techniques Used: Activity Assay

    gram positive bacteria  (ATCC)


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    ATCC gram positive bacteria
    Gram Positive Bacteria, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    miswak s mutans  (ATCC)


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    ATCC miswak s mutans
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    amycolatopsis sulphurea imet 7649t  (ATCC)


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    ATCC amycolatopsis sulphurea imet 7649t
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    amycolatopsis japonica dsm 44213 amycolatopsis thermoflava dsm 44574 amycolatopsis sulphurea atcc 27624  (ATCC)


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    ATCC amycolatopsis japonica dsm 44213 amycolatopsis thermoflava dsm 44574 amycolatopsis sulphurea atcc 27624
    Amycolatopsis Japonica Dsm 44213 Amycolatopsis Thermoflava Dsm 44574 Amycolatopsis Sulphurea Atcc 27624, 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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    t thermophilus strain hb8  (ATCC)


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    ATCC t thermophilus strain hb8
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    t thermophilus strain hb8  (ATCC)


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    ATCC t thermophilus strain hb8
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    t thermophilus strain hb8  (ATCC)


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    ATCC t thermophilus strain hb8
    T Thermophilus Strain Hb8, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    thermus thermophilus strain hb8  (ATCC)


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    ATCC thermus thermophilus strain hb8
    Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of <t> T.thermophilus </t> <t> HB8 </t> that confer thiostrepton resistance are in bold face
    Thermus Thermophilus Strain Hb8, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Thiostrepton-resistant mutants of Thermus thermophilus"

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    Journal:

    doi: 10.1093/nar/gkh644

    Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of  T.thermophilus   HB8  that confer thiostrepton resistance are in bold face
    Figure Legend Snippet: Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of T.thermophilus HB8 that confer thiostrepton resistance are in bold face

    Techniques Used: Mutagenesis

    Location of residues that were mutated in this study in the tertiary structure (2) of ribosomal protein L11 (blue) and associated 23S rRNA (orange; PDB accession code 1MMS). The putative thiostrepton-binding pocket (35) formed between the N-terminal domain (NTD) of L11 and the 23S rRNA is sufficiently large to accommodate the drug (shown in green; PDB accession code 1E9W), although not necessarily in the orientation shown here. Figure rendered with PyMOL (36). Also shown is the corresponding 23S rRNA secondary structure for part of domain II from T.thermophilus, indicating the positions of mutations described in this study. (Source: Comparative RNA website, www.rna.icmb.utexas.edu/).
    Figure Legend Snippet: Location of residues that were mutated in this study in the tertiary structure (2) of ribosomal protein L11 (blue) and associated 23S rRNA (orange; PDB accession code 1MMS). The putative thiostrepton-binding pocket (35) formed between the N-terminal domain (NTD) of L11 and the 23S rRNA is sufficiently large to accommodate the drug (shown in green; PDB accession code 1E9W), although not necessarily in the orientation shown here. Figure rendered with PyMOL (36). Also shown is the corresponding 23S rRNA secondary structure for part of domain II from T.thermophilus, indicating the positions of mutations described in this study. (Source: Comparative RNA website, www.rna.icmb.utexas.edu/).

    Techniques Used: Binding Assay

    Alignment of amino acid sequences of the L11 NTD from various organisms across all three domains of life and including mitochondrial and chloroplast L11 sequences. Positions mutated in T.thermophilus are numbered according to the E.coli sequence, and the level of conservation at these positions indicated by highlighting.
    Figure Legend Snippet: Alignment of amino acid sequences of the L11 NTD from various organisms across all three domains of life and including mitochondrial and chloroplast L11 sequences. Positions mutated in T.thermophilus are numbered according to the E.coli sequence, and the level of conservation at these positions indicated by highlighting.

    Techniques Used: Sequencing

    Pure populations of mutant rRNA as determined by primer extension analysis of 23S rRNA from thiostreptonR mutants of T.thermophilus using primers Tth1067RT (to examine mutations at position 1067 and the +G1068.1 insertion) and Tth1095RT (to examine mutations at position 1095). The wild-type sequence at each extension position is indicated on the vertical axis, with stop positions indicated in bold face. ‘Minus ddNTP’ extensions were carried out on wild-type template rRNA using all four deoxynucleotides, with no dideoxynucleotides, to reveal natural extension terminations at each position. ‘Primer only’ extensions were carried out without template rRNA, using dideoxythymidine-5′-triphosphate (ddTTP). The dideoxynucleotide termination mix used in each extension is indicated in bold face (ddCTP, dideoxycytidine-5′-triphosphate; ddATP, dideoxyadenosine-5′-triphosphate; ddTTP, dideoxythymidine-5′-triphosphate; and ddGTP, dideoxyguanosine-5′-triphosphate). The template rRNA used in each extension is indicated beneath each lane (WT, wild-type).
    Figure Legend Snippet: Pure populations of mutant rRNA as determined by primer extension analysis of 23S rRNA from thiostreptonR mutants of T.thermophilus using primers Tth1067RT (to examine mutations at position 1067 and the +G1068.1 insertion) and Tth1095RT (to examine mutations at position 1095). The wild-type sequence at each extension position is indicated on the vertical axis, with stop positions indicated in bold face. ‘Minus ddNTP’ extensions were carried out on wild-type template rRNA using all four deoxynucleotides, with no dideoxynucleotides, to reveal natural extension terminations at each position. ‘Primer only’ extensions were carried out without template rRNA, using dideoxythymidine-5′-triphosphate (ddTTP). The dideoxynucleotide termination mix used in each extension is indicated in bold face (ddCTP, dideoxycytidine-5′-triphosphate; ddATP, dideoxyadenosine-5′-triphosphate; ddTTP, dideoxythymidine-5′-triphosphate; and ddGTP, dideoxyguanosine-5′-triphosphate). The template rRNA used in each extension is indicated beneath each lane (WT, wild-type).

    Techniques Used: Mutagenesis, Sequencing

    Effect of thiostrepton on EF-G-dependent GTP hydrolysis on wild-type  T.thermophilus  and some of the thiostrepton R mutant ribosomes
    Figure Legend Snippet: Effect of thiostrepton on EF-G-dependent GTP hydrolysis on wild-type T.thermophilus and some of the thiostrepton R mutant ribosomes

    Techniques Used: Mutagenesis, Inhibition

    media thermus thermophilus strain hb8  (ATCC)


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    ATCC media thermus thermophilus strain hb8
    Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of <t> T.thermophilus </t> <t> HB8 </t> that confer thiostrepton resistance are in bold face
    Media Thermus Thermophilus Strain Hb8, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Thiostrepton-resistant mutants of Thermus thermophilus"

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    Journal:

    doi: 10.1093/nar/gkh644

    Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of  T.thermophilus   HB8  that confer thiostrepton resistance are in bold face
    Figure Legend Snippet: Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of T.thermophilus HB8 that confer thiostrepton resistance are in bold face

    Techniques Used: Mutagenesis

    Location of residues that were mutated in this study in the tertiary structure (2) of ribosomal protein L11 (blue) and associated 23S rRNA (orange; PDB accession code 1MMS). The putative thiostrepton-binding pocket (35) formed between the N-terminal domain (NTD) of L11 and the 23S rRNA is sufficiently large to accommodate the drug (shown in green; PDB accession code 1E9W), although not necessarily in the orientation shown here. Figure rendered with PyMOL (36). Also shown is the corresponding 23S rRNA secondary structure for part of domain II from T.thermophilus, indicating the positions of mutations described in this study. (Source: Comparative RNA website, www.rna.icmb.utexas.edu/).
    Figure Legend Snippet: Location of residues that were mutated in this study in the tertiary structure (2) of ribosomal protein L11 (blue) and associated 23S rRNA (orange; PDB accession code 1MMS). The putative thiostrepton-binding pocket (35) formed between the N-terminal domain (NTD) of L11 and the 23S rRNA is sufficiently large to accommodate the drug (shown in green; PDB accession code 1E9W), although not necessarily in the orientation shown here. Figure rendered with PyMOL (36). Also shown is the corresponding 23S rRNA secondary structure for part of domain II from T.thermophilus, indicating the positions of mutations described in this study. (Source: Comparative RNA website, www.rna.icmb.utexas.edu/).

    Techniques Used: Binding Assay

    Alignment of amino acid sequences of the L11 NTD from various organisms across all three domains of life and including mitochondrial and chloroplast L11 sequences. Positions mutated in T.thermophilus are numbered according to the E.coli sequence, and the level of conservation at these positions indicated by highlighting.
    Figure Legend Snippet: Alignment of amino acid sequences of the L11 NTD from various organisms across all three domains of life and including mitochondrial and chloroplast L11 sequences. Positions mutated in T.thermophilus are numbered according to the E.coli sequence, and the level of conservation at these positions indicated by highlighting.

    Techniques Used: Sequencing

    Pure populations of mutant rRNA as determined by primer extension analysis of 23S rRNA from thiostreptonR mutants of T.thermophilus using primers Tth1067RT (to examine mutations at position 1067 and the +G1068.1 insertion) and Tth1095RT (to examine mutations at position 1095). The wild-type sequence at each extension position is indicated on the vertical axis, with stop positions indicated in bold face. ‘Minus ddNTP’ extensions were carried out on wild-type template rRNA using all four deoxynucleotides, with no dideoxynucleotides, to reveal natural extension terminations at each position. ‘Primer only’ extensions were carried out without template rRNA, using dideoxythymidine-5′-triphosphate (ddTTP). The dideoxynucleotide termination mix used in each extension is indicated in bold face (ddCTP, dideoxycytidine-5′-triphosphate; ddATP, dideoxyadenosine-5′-triphosphate; ddTTP, dideoxythymidine-5′-triphosphate; and ddGTP, dideoxyguanosine-5′-triphosphate). The template rRNA used in each extension is indicated beneath each lane (WT, wild-type).
    Figure Legend Snippet: Pure populations of mutant rRNA as determined by primer extension analysis of 23S rRNA from thiostreptonR mutants of T.thermophilus using primers Tth1067RT (to examine mutations at position 1067 and the +G1068.1 insertion) and Tth1095RT (to examine mutations at position 1095). The wild-type sequence at each extension position is indicated on the vertical axis, with stop positions indicated in bold face. ‘Minus ddNTP’ extensions were carried out on wild-type template rRNA using all four deoxynucleotides, with no dideoxynucleotides, to reveal natural extension terminations at each position. ‘Primer only’ extensions were carried out without template rRNA, using dideoxythymidine-5′-triphosphate (ddTTP). The dideoxynucleotide termination mix used in each extension is indicated in bold face (ddCTP, dideoxycytidine-5′-triphosphate; ddATP, dideoxyadenosine-5′-triphosphate; ddTTP, dideoxythymidine-5′-triphosphate; and ddGTP, dideoxyguanosine-5′-triphosphate). The template rRNA used in each extension is indicated beneath each lane (WT, wild-type).

    Techniques Used: Mutagenesis, Sequencing

    Effect of thiostrepton on EF-G-dependent GTP hydrolysis on wild-type  T.thermophilus  and some of the thiostrepton R mutant ribosomes
    Figure Legend Snippet: Effect of thiostrepton on EF-G-dependent GTP hydrolysis on wild-type T.thermophilus and some of the thiostrepton R mutant ribosomes

    Techniques Used: Mutagenesis, Inhibition

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    ATCC thermus thermophilus strain hb8
    Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of <t> T.thermophilus </t> <t> HB8 </t> that confer thiostrepton resistance are in bold face
    Thermus Thermophilus Strain Hb8, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC media thermus thermophilus strain hb8
    Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of <t> T.thermophilus </t> <t> HB8 </t> that confer thiostrepton resistance are in bold face
    Media Thermus Thermophilus Strain Hb8, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/media thermus thermophilus strain hb8/product/ATCC
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    media thermus thermophilus strain hb8 - by Bioz Stars, 2024-02
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    Image Search Results


    Anti-microbial activity of clinical working concentrations of PHMG-P (1%) and CHX (0.2%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).

    Journal: Annals of Clinical Microbiology and Antimicrobials

    Article Title: Antimicrobial activity of polyhexamethylene guanidine phosphate in comparison to chlorhexidine using the quantitative suspension method

    doi: 10.1186/s12941-015-0097-x

    Figure Lengend Snippet: Anti-microbial activity of clinical working concentrations of PHMG-P (1%) and CHX (0.2%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).

    Article Snippet: Anti-bacterial activity of antiseptics was estimated on the following standard strains of Staphylococcus aureus (ATCC 6538), Escherichia coli (ATCC 11229), Pseudomonas aeruginosa (ATCC 15412), and Candida albicans (ATCC 1023), and on the oral Gram-negative periodontal pathogens Porphyromonas gingivalis (ATCC 33277), Aggregatibacter actinomycetemcomitans (HK 1519), Gram-positive cariogenic strains Streptococcus mutans (CCUG 27624; Ing-Brit), and Lactobacillus acidophilus (NCTC 1723).

    Techniques: Activity Assay

    Anti-microbial activity of highly diluted PHMG-P (0.05%) and CHX (0.05%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).

    Journal: Annals of Clinical Microbiology and Antimicrobials

    Article Title: Antimicrobial activity of polyhexamethylene guanidine phosphate in comparison to chlorhexidine using the quantitative suspension method

    doi: 10.1186/s12941-015-0097-x

    Figure Lengend Snippet: Anti-microbial activity of highly diluted PHMG-P (0.05%) and CHX (0.05%) against perio- and cariogenic bacteria ( P. gingivalis , A. actinomycetemcomitans , S. mutans and L. acidophilus ).

    Article Snippet: Anti-bacterial activity of antiseptics was estimated on the following standard strains of Staphylococcus aureus (ATCC 6538), Escherichia coli (ATCC 11229), Pseudomonas aeruginosa (ATCC 15412), and Candida albicans (ATCC 1023), and on the oral Gram-negative periodontal pathogens Porphyromonas gingivalis (ATCC 33277), Aggregatibacter actinomycetemcomitans (HK 1519), Gram-positive cariogenic strains Streptococcus mutans (CCUG 27624; Ing-Brit), and Lactobacillus acidophilus (NCTC 1723).

    Techniques: Activity Assay

    Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of  T.thermophilus   HB8  that confer thiostrepton resistance are in bold face

    Journal:

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    doi: 10.1093/nar/gkh644

    Figure Lengend Snippet: Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of T.thermophilus HB8 that confer thiostrepton resistance are in bold face

    Article Snippet: Thermus thermophilus strain HB8 ( 18 ) (ATCC 27624) was obtained from the American Type Culture Collection (ATCC).

    Techniques: Mutagenesis

    Location of residues that were mutated in this study in the tertiary structure (2) of ribosomal protein L11 (blue) and associated 23S rRNA (orange; PDB accession code 1MMS). The putative thiostrepton-binding pocket (35) formed between the N-terminal domain (NTD) of L11 and the 23S rRNA is sufficiently large to accommodate the drug (shown in green; PDB accession code 1E9W), although not necessarily in the orientation shown here. Figure rendered with PyMOL (36). Also shown is the corresponding 23S rRNA secondary structure for part of domain II from T.thermophilus, indicating the positions of mutations described in this study. (Source: Comparative RNA website, www.rna.icmb.utexas.edu/).

    Journal:

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    doi: 10.1093/nar/gkh644

    Figure Lengend Snippet: Location of residues that were mutated in this study in the tertiary structure (2) of ribosomal protein L11 (blue) and associated 23S rRNA (orange; PDB accession code 1MMS). The putative thiostrepton-binding pocket (35) formed between the N-terminal domain (NTD) of L11 and the 23S rRNA is sufficiently large to accommodate the drug (shown in green; PDB accession code 1E9W), although not necessarily in the orientation shown here. Figure rendered with PyMOL (36). Also shown is the corresponding 23S rRNA secondary structure for part of domain II from T.thermophilus, indicating the positions of mutations described in this study. (Source: Comparative RNA website, www.rna.icmb.utexas.edu/).

    Article Snippet: Thermus thermophilus strain HB8 ( 18 ) (ATCC 27624) was obtained from the American Type Culture Collection (ATCC).

    Techniques: Binding Assay

    Alignment of amino acid sequences of the L11 NTD from various organisms across all three domains of life and including mitochondrial and chloroplast L11 sequences. Positions mutated in T.thermophilus are numbered according to the E.coli sequence, and the level of conservation at these positions indicated by highlighting.

    Journal:

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    doi: 10.1093/nar/gkh644

    Figure Lengend Snippet: Alignment of amino acid sequences of the L11 NTD from various organisms across all three domains of life and including mitochondrial and chloroplast L11 sequences. Positions mutated in T.thermophilus are numbered according to the E.coli sequence, and the level of conservation at these positions indicated by highlighting.

    Article Snippet: Thermus thermophilus strain HB8 ( 18 ) (ATCC 27624) was obtained from the American Type Culture Collection (ATCC).

    Techniques: Sequencing

    Pure populations of mutant rRNA as determined by primer extension analysis of 23S rRNA from thiostreptonR mutants of T.thermophilus using primers Tth1067RT (to examine mutations at position 1067 and the +G1068.1 insertion) and Tth1095RT (to examine mutations at position 1095). The wild-type sequence at each extension position is indicated on the vertical axis, with stop positions indicated in bold face. ‘Minus ddNTP’ extensions were carried out on wild-type template rRNA using all four deoxynucleotides, with no dideoxynucleotides, to reveal natural extension terminations at each position. ‘Primer only’ extensions were carried out without template rRNA, using dideoxythymidine-5′-triphosphate (ddTTP). The dideoxynucleotide termination mix used in each extension is indicated in bold face (ddCTP, dideoxycytidine-5′-triphosphate; ddATP, dideoxyadenosine-5′-triphosphate; ddTTP, dideoxythymidine-5′-triphosphate; and ddGTP, dideoxyguanosine-5′-triphosphate). The template rRNA used in each extension is indicated beneath each lane (WT, wild-type).

    Journal:

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    doi: 10.1093/nar/gkh644

    Figure Lengend Snippet: Pure populations of mutant rRNA as determined by primer extension analysis of 23S rRNA from thiostreptonR mutants of T.thermophilus using primers Tth1067RT (to examine mutations at position 1067 and the +G1068.1 insertion) and Tth1095RT (to examine mutations at position 1095). The wild-type sequence at each extension position is indicated on the vertical axis, with stop positions indicated in bold face. ‘Minus ddNTP’ extensions were carried out on wild-type template rRNA using all four deoxynucleotides, with no dideoxynucleotides, to reveal natural extension terminations at each position. ‘Primer only’ extensions were carried out without template rRNA, using dideoxythymidine-5′-triphosphate (ddTTP). The dideoxynucleotide termination mix used in each extension is indicated in bold face (ddCTP, dideoxycytidine-5′-triphosphate; ddATP, dideoxyadenosine-5′-triphosphate; ddTTP, dideoxythymidine-5′-triphosphate; and ddGTP, dideoxyguanosine-5′-triphosphate). The template rRNA used in each extension is indicated beneath each lane (WT, wild-type).

    Article Snippet: Thermus thermophilus strain HB8 ( 18 ) (ATCC 27624) was obtained from the American Type Culture Collection (ATCC).

    Techniques: Mutagenesis, Sequencing

    Effect of thiostrepton on EF-G-dependent GTP hydrolysis on wild-type  T.thermophilus  and some of the thiostrepton R mutant ribosomes

    Journal:

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    doi: 10.1093/nar/gkh644

    Figure Lengend Snippet: Effect of thiostrepton on EF-G-dependent GTP hydrolysis on wild-type T.thermophilus and some of the thiostrepton R mutant ribosomes

    Article Snippet: Thermus thermophilus strain HB8 ( 18 ) (ATCC 27624) was obtained from the American Type Culture Collection (ATCC).

    Techniques: Mutagenesis, Inhibition

    Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of  T.thermophilus   HB8  that confer thiostrepton resistance are in bold face

    Journal:

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    doi: 10.1093/nar/gkh644

    Figure Lengend Snippet: Mutations identified in this study in the rplK (L11) and rrl (23S rRNA) genes of T.thermophilus HB8 that confer thiostrepton resistance are in bold face

    Article Snippet: Bacterial strains and media Thermus thermophilus strain HB8 ( 18 ) (ATCC 27624) was obtained from the American Type Culture Collection (ATCC).

    Techniques: Mutagenesis

    Location of residues that were mutated in this study in the tertiary structure (2) of ribosomal protein L11 (blue) and associated 23S rRNA (orange; PDB accession code 1MMS). The putative thiostrepton-binding pocket (35) formed between the N-terminal domain (NTD) of L11 and the 23S rRNA is sufficiently large to accommodate the drug (shown in green; PDB accession code 1E9W), although not necessarily in the orientation shown here. Figure rendered with PyMOL (36). Also shown is the corresponding 23S rRNA secondary structure for part of domain II from T.thermophilus, indicating the positions of mutations described in this study. (Source: Comparative RNA website, www.rna.icmb.utexas.edu/).

    Journal:

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    doi: 10.1093/nar/gkh644

    Figure Lengend Snippet: Location of residues that were mutated in this study in the tertiary structure (2) of ribosomal protein L11 (blue) and associated 23S rRNA (orange; PDB accession code 1MMS). The putative thiostrepton-binding pocket (35) formed between the N-terminal domain (NTD) of L11 and the 23S rRNA is sufficiently large to accommodate the drug (shown in green; PDB accession code 1E9W), although not necessarily in the orientation shown here. Figure rendered with PyMOL (36). Also shown is the corresponding 23S rRNA secondary structure for part of domain II from T.thermophilus, indicating the positions of mutations described in this study. (Source: Comparative RNA website, www.rna.icmb.utexas.edu/).

    Article Snippet: Bacterial strains and media Thermus thermophilus strain HB8 ( 18 ) (ATCC 27624) was obtained from the American Type Culture Collection (ATCC).

    Techniques: Binding Assay

    Alignment of amino acid sequences of the L11 NTD from various organisms across all three domains of life and including mitochondrial and chloroplast L11 sequences. Positions mutated in T.thermophilus are numbered according to the E.coli sequence, and the level of conservation at these positions indicated by highlighting.

    Journal:

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    doi: 10.1093/nar/gkh644

    Figure Lengend Snippet: Alignment of amino acid sequences of the L11 NTD from various organisms across all three domains of life and including mitochondrial and chloroplast L11 sequences. Positions mutated in T.thermophilus are numbered according to the E.coli sequence, and the level of conservation at these positions indicated by highlighting.

    Article Snippet: Bacterial strains and media Thermus thermophilus strain HB8 ( 18 ) (ATCC 27624) was obtained from the American Type Culture Collection (ATCC).

    Techniques: Sequencing

    Pure populations of mutant rRNA as determined by primer extension analysis of 23S rRNA from thiostreptonR mutants of T.thermophilus using primers Tth1067RT (to examine mutations at position 1067 and the +G1068.1 insertion) and Tth1095RT (to examine mutations at position 1095). The wild-type sequence at each extension position is indicated on the vertical axis, with stop positions indicated in bold face. ‘Minus ddNTP’ extensions were carried out on wild-type template rRNA using all four deoxynucleotides, with no dideoxynucleotides, to reveal natural extension terminations at each position. ‘Primer only’ extensions were carried out without template rRNA, using dideoxythymidine-5′-triphosphate (ddTTP). The dideoxynucleotide termination mix used in each extension is indicated in bold face (ddCTP, dideoxycytidine-5′-triphosphate; ddATP, dideoxyadenosine-5′-triphosphate; ddTTP, dideoxythymidine-5′-triphosphate; and ddGTP, dideoxyguanosine-5′-triphosphate). The template rRNA used in each extension is indicated beneath each lane (WT, wild-type).

    Journal:

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    doi: 10.1093/nar/gkh644

    Figure Lengend Snippet: Pure populations of mutant rRNA as determined by primer extension analysis of 23S rRNA from thiostreptonR mutants of T.thermophilus using primers Tth1067RT (to examine mutations at position 1067 and the +G1068.1 insertion) and Tth1095RT (to examine mutations at position 1095). The wild-type sequence at each extension position is indicated on the vertical axis, with stop positions indicated in bold face. ‘Minus ddNTP’ extensions were carried out on wild-type template rRNA using all four deoxynucleotides, with no dideoxynucleotides, to reveal natural extension terminations at each position. ‘Primer only’ extensions were carried out without template rRNA, using dideoxythymidine-5′-triphosphate (ddTTP). The dideoxynucleotide termination mix used in each extension is indicated in bold face (ddCTP, dideoxycytidine-5′-triphosphate; ddATP, dideoxyadenosine-5′-triphosphate; ddTTP, dideoxythymidine-5′-triphosphate; and ddGTP, dideoxyguanosine-5′-triphosphate). The template rRNA used in each extension is indicated beneath each lane (WT, wild-type).

    Article Snippet: Bacterial strains and media Thermus thermophilus strain HB8 ( 18 ) (ATCC 27624) was obtained from the American Type Culture Collection (ATCC).

    Techniques: Mutagenesis, Sequencing

    Effect of thiostrepton on EF-G-dependent GTP hydrolysis on wild-type  T.thermophilus  and some of the thiostrepton R mutant ribosomes

    Journal:

    Article Title: Thiostrepton-resistant mutants of Thermus thermophilus

    doi: 10.1093/nar/gkh644

    Figure Lengend Snippet: Effect of thiostrepton on EF-G-dependent GTP hydrolysis on wild-type T.thermophilus and some of the thiostrepton R mutant ribosomes

    Article Snippet: Bacterial strains and media Thermus thermophilus strain HB8 ( 18 ) (ATCC 27624) was obtained from the American Type Culture Collection (ATCC).

    Techniques: Mutagenesis, Inhibition