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The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD(2)-(c-di-GMP)(4) complex
Streptomyces are ubiquitous soil bacteria that undergo a complex developmental transition coinciding with their production of antibiotics. This transition is controlled by binding of a novel tetrameric form of the second messenger, 3΄-5΄ cyclic diguanylic acid (c-di-GMP) to the master repressor, Bld...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5499655/ https://www.ncbi.nlm.nih.gov/pubmed/28449057 http://dx.doi.org/10.1093/nar/gkx287 |
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author | Schumacher, Maria A. Zeng, Wenjie Findlay, Kim C. Buttner, Mark J. Brennan, Richard G. Tschowri, Natalia |
author_facet | Schumacher, Maria A. Zeng, Wenjie Findlay, Kim C. Buttner, Mark J. Brennan, Richard G. Tschowri, Natalia |
author_sort | Schumacher, Maria A. |
collection | PubMed |
description | Streptomyces are ubiquitous soil bacteria that undergo a complex developmental transition coinciding with their production of antibiotics. This transition is controlled by binding of a novel tetrameric form of the second messenger, 3΄-5΄ cyclic diguanylic acid (c-di-GMP) to the master repressor, BldD. In all domains of life, nucleotide-based second messengers allow a rapid integration of external and internal signals into regulatory pathways that control cellular responses to changing conditions. c-di-GMP can assume alternative oligomeric states to effect different functions, binding to effector proteins as monomers, intercalated dimers or, uniquely in the case of BldD, as a tetramer. However, at physiological concentrations c-di-GMP is a monomer and little is known about how higher oligomeric complexes assemble on effector proteins and if intermediates in assembly pathways have regulatory significance. Here, we show that c-di-GMP binds BldD using an ordered, sequential mechanism and that BldD function necessitates the assembly of the BldD(2)-(c-di-GMP)(4) complex. |
format | Online Article Text |
id | pubmed-5499655 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-54996552017-07-10 The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD(2)-(c-di-GMP)(4) complex Schumacher, Maria A. Zeng, Wenjie Findlay, Kim C. Buttner, Mark J. Brennan, Richard G. Tschowri, Natalia Nucleic Acids Res Structural Biology Streptomyces are ubiquitous soil bacteria that undergo a complex developmental transition coinciding with their production of antibiotics. This transition is controlled by binding of a novel tetrameric form of the second messenger, 3΄-5΄ cyclic diguanylic acid (c-di-GMP) to the master repressor, BldD. In all domains of life, nucleotide-based second messengers allow a rapid integration of external and internal signals into regulatory pathways that control cellular responses to changing conditions. c-di-GMP can assume alternative oligomeric states to effect different functions, binding to effector proteins as monomers, intercalated dimers or, uniquely in the case of BldD, as a tetramer. However, at physiological concentrations c-di-GMP is a monomer and little is known about how higher oligomeric complexes assemble on effector proteins and if intermediates in assembly pathways have regulatory significance. Here, we show that c-di-GMP binds BldD using an ordered, sequential mechanism and that BldD function necessitates the assembly of the BldD(2)-(c-di-GMP)(4) complex. Oxford University Press 2017-06-20 2017-04-26 /pmc/articles/PMC5499655/ /pubmed/28449057 http://dx.doi.org/10.1093/nar/gkx287 Text en © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Structural Biology Schumacher, Maria A. Zeng, Wenjie Findlay, Kim C. Buttner, Mark J. Brennan, Richard G. Tschowri, Natalia The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD(2)-(c-di-GMP)(4) complex |
title | The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD(2)-(c-di-GMP)(4) complex |
title_full | The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD(2)-(c-di-GMP)(4) complex |
title_fullStr | The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD(2)-(c-di-GMP)(4) complex |
title_full_unstemmed | The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD(2)-(c-di-GMP)(4) complex |
title_short | The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD(2)-(c-di-GMP)(4) complex |
title_sort | streptomyces master regulator bldd binds c-di-gmp sequentially to create a functional bldd(2)-(c-di-gmp)(4) complex |
topic | Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5499655/ https://www.ncbi.nlm.nih.gov/pubmed/28449057 http://dx.doi.org/10.1093/nar/gkx287 |
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