Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-03576-3
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Funding
- BBSRC [BB/H006125/1]
- BBSRC Institute Strategic Programme Grant [BB/J004561/1]
- National Institutes of Health [GM115547]
- National Institutes of Health
- National Institute of General Medical Sciences
- Howard Hughes Medical Institute
- Office of Science, Office of Basic Energy Sciences, of the U.S. Department of Energy [DE-AC02-05CH11231]
- University of California Office of the President, Multicampus Research Programs, and Initiatives grant [MR-15-328599]
- Sandler Foundation
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R35GM130290, R01GM115547] Funding Source: NIH RePORTER
- BBSRC [BBS/E/J/000PR9791] Funding Source: UKRI
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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.
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