The MerR-like protein BldC binds DNA direct repeats as cooperative multimers to regulate Streptomyces development
Abstract
Streptomycetes are notable for their complex life cycle and production of most clinically important antibiotics. A key factor that controls entry into development and the onset of antibiotic production is the 68-residue protein, BldC. BldC is a putative DNA-binding protein related to MerR regulators, but lacks coiled-coil dimerization and effector-binding domains characteristic of classical MerR proteins. Hence, the molecular function of the protein has been unclear. Here we show that BldC is indeed a DNA-binding protein and controls a regulon that includes other key developmental regulators. Intriguingly, BldC DNA-binding sites vary significantly in length. Our BldC-DNA structures explain this DNA-binding capability by revealing that BldC utilizes a DNA-binding mode distinct from MerR and other known regulators, involving asymmetric head-to-tail oligomerization on DNA direct repeats that results in dramatic DNA distortion. Notably, BldC-like proteins radiate throughout eubacteria, establishing BldC as the founding member of a new structural family of regulators.
- Authors:
-
[2];
- Duke Univ. School of Medicine, Durham, NC (United States). Dept. of Biochemistry
- John Innes Centre (United Kingdom). Dept. of Molecular Microbiology
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1624083
- Grant/Contract Number:
- AC02-05CH11231
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 9; Journal Issue: 1; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- Science & Technology - Other Topics
Citation Formats
Schumacher, Maria A., den Hengst, Chris D., Bush, Matthew J., Le, T. B. K., Tran, Ngat T., Chandra, Govind, Zeng, Wenjie, Travis, Brady, Brennan, Richard G., and Buttner, Mark J. The MerR-like protein BldC binds DNA direct repeats as cooperative multimers to regulate Streptomyces development. United States: N. p., 2018.
Web. doi:10.1038/s41467-018-03576-3.
Schumacher, Maria A., den Hengst, Chris D., Bush, Matthew J., Le, T. B. K., Tran, Ngat T., Chandra, Govind, Zeng, Wenjie, Travis, Brady, Brennan, Richard G., & Buttner, Mark J. The MerR-like protein BldC binds DNA direct repeats as cooperative multimers to regulate Streptomyces development. United States. https://doi.org/10.1038/s41467-018-03576-3
Schumacher, Maria A., den Hengst, Chris D., Bush, Matthew J., Le, T. B. K., Tran, Ngat T., Chandra, Govind, Zeng, Wenjie, Travis, Brady, Brennan, Richard G., and Buttner, Mark J. Mon .
"The MerR-like protein BldC binds DNA direct repeats as cooperative multimers to regulate Streptomyces development". United States. https://doi.org/10.1038/s41467-018-03576-3. https://www.osti.gov/servlets/purl/1624083.
@article{osti_1624083,
title = {The MerR-like protein BldC binds DNA direct repeats as cooperative multimers to regulate Streptomyces development},
author = {Schumacher, Maria A. and den Hengst, Chris D. and Bush, Matthew J. and Le, T. B. K. and Tran, Ngat T. and Chandra, Govind and Zeng, Wenjie and Travis, Brady and Brennan, Richard G. and Buttner, Mark J.},
abstractNote = {Streptomycetes are notable for their complex life cycle and production of most clinically important antibiotics. A key factor that controls entry into development and the onset of antibiotic production is the 68-residue protein, BldC. BldC is a putative DNA-binding protein related to MerR regulators, but lacks coiled-coil dimerization and effector-binding domains characteristic of classical MerR proteins. Hence, the molecular function of the protein has been unclear. Here we show that BldC is indeed a DNA-binding protein and controls a regulon that includes other key developmental regulators. Intriguingly, BldC DNA-binding sites vary significantly in length. Our BldC-DNA structures explain this DNA-binding capability by revealing that BldC utilizes a DNA-binding mode distinct from MerR and other known regulators, involving asymmetric head-to-tail oligomerization on DNA direct repeats that results in dramatic DNA distortion. Notably, BldC-like proteins radiate throughout eubacteria, establishing BldC as the founding member of a new structural family of regulators.},
doi = {10.1038/s41467-018-03576-3},
journal = {Nature Communications},
number = 1,
volume = 9,
place = {United States},
year = {Mon Mar 19 00:00:00 EDT 2018},
month = {Mon Mar 19 00:00:00 EDT 2018}
}
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