The heptameric structure of the flagellar regulatory protein FlrC is indispensable for ATPase activity and disassembled by cyclic-di-GMP.

ABSTRACT: The bacterial enhancer-binding protein (bEBP) FlrC, controls motility and colonization of Vibrio cholerae by regulating the transcription of class-III flagellar genes in σ⁵⁴-dependent manner. However, the mechanism by which FlrC regulates transcription is not fully elucidated. Although, most bEBPs require nucleotides to stimulate the oligomerization necessary for function, our previous study showed that the central domain of FlrC (FlrC^C) forms heptamer in a nucleotide-independent manner. Furthermore, heptameric FlrC^C binds ATP in "cis-mediated" style without any contribution from sensor I motif ²⁸⁵REDXXYR²⁹¹ of the trans protomer. This atypical ATP binding raises the question of whether heptamerization of FlrC is s

SUBMITTER: Chakraborty S 

PROVIDER: S-EPMC7863884 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature