An autoinhibitory mechanism controls RNA-binding activity of the nitrate-sensing protein NasR.

ABSTRACT: The ANTAR domain harnesses RNA-binding activity to promote transcription attenuation. Although several ANTAR proteins have been analyzed by high-resolution structural analyses, the residues involved in RNA-recognition and transcription attenuation have not been identified. Nor is it clear how signal-responsive domains are allosterically coupled with ANTAR domains for control of gene expression. Herein, we examined the sequence conservation of ANTAR domains to find residues that may associate with RNA. We subjected the corresponding positions of Klebsiella oxytoca NasR to site-directed alanine substitutions and measured RNA-binding activity. This revealed a functionally important patch of residues that forms amino acid pairing interactions with residues from NasR's nitrate-sensing NIT domai

SUBMITTER: Goodson JR 

PROVIDER: S-EPMC7496416 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature