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Reduced synthesis of the Ybt siderophore or production of aberrant Ybt-like molecules activates transcription of yersiniabactin genes in Yersinia pestis

Synthesis of the siderophore yersiniabactin (Ybt) proceeds by a mixed nonribosomal peptide synthetase/polyketide synthase mechanism. Transcription of ybt genes encoding biosynthetic and transport functions is repressed under excess iron conditions by Fur, but is also activated by Ybt via the transcr...

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Autores principales: Miller, M. Clarke, Fetherston, Jacqueline D., Pickett, Carol L., Bobrov, Alexander G., Weaver, Robert H., DeMoll, Edward, Perry, Robert D.
Formato: Texto
Lenguaje:English
Publicado: Microbiology Society 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3068685/
https://www.ncbi.nlm.nih.gov/pubmed/20413552
http://dx.doi.org/10.1099/mic.0.037945-0
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author Miller, M. Clarke
Fetherston, Jacqueline D.
Pickett, Carol L.
Bobrov, Alexander G.
Weaver, Robert H.
DeMoll, Edward
Perry, Robert D.
author_facet Miller, M. Clarke
Fetherston, Jacqueline D.
Pickett, Carol L.
Bobrov, Alexander G.
Weaver, Robert H.
DeMoll, Edward
Perry, Robert D.
author_sort Miller, M. Clarke
collection PubMed
description Synthesis of the siderophore yersiniabactin (Ybt) proceeds by a mixed nonribosomal peptide synthetase/polyketide synthase mechanism. Transcription of ybt genes encoding biosynthetic and transport functions is repressed under excess iron conditions by Fur, but is also activated by Ybt via the transcriptional regulator YbtA. While mutations in most biosynthetic genes and ybtA negate transcription activation from the regulated promoters, three biosynthetic mutations do not reduce this transcriptional activation. Here we show that two of these mutants, one lacking the putative type II thioesterase (TE) YbtT and the other with a mutation in the TE domain of HMWP1, produce reduced levels of authentic Ybt that are capable of signalling activity. Alanine substitutions in two residues of YbtT that are essential for catalytic activity in other type II TEs reduced the ability of Yersinia pestis to grow under iron-chelated conditions. The third mutant, which lacks the salicylate synthase YbtS, did not make authentic Ybt but did produce a signalling molecule. Finally, a Δpgm strain of Y. pestis, which lacks essential Ybt biosynthetic genes, also produced a signalling molecule that can activate transcription of ybt genes. The non-Ybt signal molecules from these two mutants are likely separate compounds. While these compounds are not biologically relevant to normal Ybt regulation, a comparison of the structures of Ybt and other signalling molecules will help in determining the chemical structures recognized as a Ybt signal.
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spelling pubmed-30686852011-07-01 Reduced synthesis of the Ybt siderophore or production of aberrant Ybt-like molecules activates transcription of yersiniabactin genes in Yersinia pestis Miller, M. Clarke Fetherston, Jacqueline D. Pickett, Carol L. Bobrov, Alexander G. Weaver, Robert H. DeMoll, Edward Perry, Robert D. Microbiology (Reading) Microbial Pathogenicity Synthesis of the siderophore yersiniabactin (Ybt) proceeds by a mixed nonribosomal peptide synthetase/polyketide synthase mechanism. Transcription of ybt genes encoding biosynthetic and transport functions is repressed under excess iron conditions by Fur, but is also activated by Ybt via the transcriptional regulator YbtA. While mutations in most biosynthetic genes and ybtA negate transcription activation from the regulated promoters, three biosynthetic mutations do not reduce this transcriptional activation. Here we show that two of these mutants, one lacking the putative type II thioesterase (TE) YbtT and the other with a mutation in the TE domain of HMWP1, produce reduced levels of authentic Ybt that are capable of signalling activity. Alanine substitutions in two residues of YbtT that are essential for catalytic activity in other type II TEs reduced the ability of Yersinia pestis to grow under iron-chelated conditions. The third mutant, which lacks the salicylate synthase YbtS, did not make authentic Ybt but did produce a signalling molecule. Finally, a Δpgm strain of Y. pestis, which lacks essential Ybt biosynthetic genes, also produced a signalling molecule that can activate transcription of ybt genes. The non-Ybt signal molecules from these two mutants are likely separate compounds. While these compounds are not biologically relevant to normal Ybt regulation, a comparison of the structures of Ybt and other signalling molecules will help in determining the chemical structures recognized as a Ybt signal. Microbiology Society 2010-07 /pmc/articles/PMC3068685/ /pubmed/20413552 http://dx.doi.org/10.1099/mic.0.037945-0 Text en Copyright © 2010, SGM
spellingShingle Microbial Pathogenicity
Miller, M. Clarke
Fetherston, Jacqueline D.
Pickett, Carol L.
Bobrov, Alexander G.
Weaver, Robert H.
DeMoll, Edward
Perry, Robert D.
Reduced synthesis of the Ybt siderophore or production of aberrant Ybt-like molecules activates transcription of yersiniabactin genes in Yersinia pestis
title Reduced synthesis of the Ybt siderophore or production of aberrant Ybt-like molecules activates transcription of yersiniabactin genes in Yersinia pestis
title_full Reduced synthesis of the Ybt siderophore or production of aberrant Ybt-like molecules activates transcription of yersiniabactin genes in Yersinia pestis
title_fullStr Reduced synthesis of the Ybt siderophore or production of aberrant Ybt-like molecules activates transcription of yersiniabactin genes in Yersinia pestis
title_full_unstemmed Reduced synthesis of the Ybt siderophore or production of aberrant Ybt-like molecules activates transcription of yersiniabactin genes in Yersinia pestis
title_short Reduced synthesis of the Ybt siderophore or production of aberrant Ybt-like molecules activates transcription of yersiniabactin genes in Yersinia pestis
title_sort reduced synthesis of the ybt siderophore or production of aberrant ybt-like molecules activates transcription of yersiniabactin genes in yersinia pestis
topic Microbial Pathogenicity
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3068685/
https://www.ncbi.nlm.nih.gov/pubmed/20413552
http://dx.doi.org/10.1099/mic.0.037945-0
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