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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...

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Autores principales: Schumacher, Maria A., Zeng, Wenjie, Findlay, Kim C., Buttner, Mark J., Brennan, Richard G., Tschowri, Natalia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2017
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.
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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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