An NMR Study on the clpC Operon Binding Region of Transcription Factor CtsR from Bacillus subtilis

Abstract

When Gram-positive bacterium Bacillus subtilis responds to heat-shock, protein arginine kinase McsB phosphorylates Arg62 (R) in the clpC operon binding region of transcription factor CtsR, leading to dissociation of CtsR and clpC operon and initiation of stress-genes transcription for the ensuing expression of heat-shock proteins. This work investigated the clpC operon binding region (KRGGGG) of CtsR with NMR spectra (i.e., 1H NMR, 1H-1H COSY, 1H-1H TOCSY, 1H-15N HSQC and 1H-13C HSQC). The 1H, 13C and 15N chemical shifts of the protein segment were assigned. The interaction between CtsR and clpC operon and the regulatory mechanism of arginine phosphorylation were analyzed.

Keywords

• transcription factor
• nuclear magnetic resonance (nmr)
• chemical shifts
• structure in solution