An increase in surface hydrophobicity mediates chaperone activity in N-chlorinated RidA.

ABSTRACT: Under physiological conditions, Escherichia coli RidA is an enamine/imine deaminase, which promotes the release of ammonia from reactive enamine/imine intermediates. However, when modified by hypochlorous acid (HOCl), it turns into a potent chaperone-like holdase that can effectively protect E. coli's proteome during oxidative stress. However, it is unknown, which residues need to be chlorinated for activation. Here, we employ a combination of LC-MS/MS analysis, a chemo-proteomic approach, and a mutagenesis study to identify residues responsible for RidA's chaperone-like function. Through LC-MS/MS of digested RidA_HOCl, we obtained direct evidence of the chlorination of one arginine residue. To overcome the instability of the N-chloramine modification, we established a chemoprote

SUBMITTER: Varatnitskaya M 

PROVIDER: S-EPMC9126958 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature