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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Schumacher MA,den Hengst CD,Bush MJ,Le TBK,Tran NT,Chandra G,Zeng W,Travis B,Brennan RG,Buttner MJdoi
10.1038/s41467-018-03576-3subject
Has Abstractpub_date
2018-03-19 00:00:00pages
1139issue
1issn
2041-1723pii
10.1038/s41467-018-03576-3journal_volume
9pub_type
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