Details
| Original language | English |
|---|---|
| Pages (from-to) | 6923-6933 |
| Number of pages | 11 |
| Journal | Nucleic acids research |
| Volume | 45 |
| Issue number | 11 |
| Publication status | Published - 20 Jun 2017 |
| Externally published | Yes |
Abstract
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 BldD2-(c-di-GMP)4 complex.
Keywords
- Bacterial Proteins/chemistry, Binding Sites, Crystallography, X-Ray, Cyclic GMP/analogs & derivatives, Hydrogen Bonding, Models, Molecular, Protein Binding, Protein Domains, Protein Stability, Protein Structure, Quaternary, Repressor Proteins/chemistry, Streptomyces
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
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In: Nucleic acids research, Vol. 45, No. 11, 20.06.2017, p. 6923-6933.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD2-(c-di-GMP)4 complex
AU - Schumacher, Maria A
AU - Zeng, Wenjie
AU - Findlay, Kim C
AU - Buttner, Mark J
AU - Brennan, Richard G
AU - Tschowri, Natalia
N1 - Publisher Copyright: © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2017/6/20
Y1 - 2017/6/20
N2 - 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 BldD2-(c-di-GMP)4 complex.
AB - 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 BldD2-(c-di-GMP)4 complex.
KW - Bacterial Proteins/chemistry
KW - Binding Sites
KW - Crystallography, X-Ray
KW - Cyclic GMP/analogs & derivatives
KW - Hydrogen Bonding
KW - Models, Molecular
KW - Protein Binding
KW - Protein Domains
KW - Protein Stability
KW - Protein Structure, Quaternary
KW - Repressor Proteins/chemistry
KW - Streptomyces
UR - http://www.scopus.com/inward/record.url?scp=85027247495&partnerID=8YFLogxK
U2 - 10.1093/nar/gkx287
DO - 10.1093/nar/gkx287
M3 - Article
C2 - 28449057
VL - 45
SP - 6923
EP - 6933
JO - Nucleic acids research
JF - Nucleic acids research
SN - 0301-5610
IS - 11
ER -