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Publication Abstract from PubMed

In mycobacteria, transcriptional activator PafBC is responsible for upregulating the majority of genes induced by DNA damage. Understanding the mechanism of PafBC activation is impeded by a lack of structural information on this transcription factor that contains a widespread, but poorly understood WYL domain frequently encountered in bacterial transcription factors. Here, we determine the crystal structure of Arthrobacter aurescens PafBC. The protein consists of two modules, each harboring an N-terminal helix-turn-helix DNA-binding domain followed by a central WYL and a C-terminal extension (WCX) domain. The WYL domains exhibit Sm-folds, while the WCX domains adopt ferredoxin-like folds, both characteristic for RNA-binding proteins. Our results suggest a mechanism of regulation in which WYL domain-containing transcription factors may be activated by binding RNA or other nucleic acid molecules. Using an in vivo mutational screen in Mycobacterium smegmatis, we identify potential co-activator binding sites on PafBC.

Structure and functional implications of WYL domain-containing bacterial DNA damage response regulator PafBC.,Muller AU, Leibundgut M, Ban N, Weber-Ban E Nat Commun. 2019 Oct 11;10(1):4653. doi: 10.1038/s41467-019-12567-x. PMID:31604936^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.