Activation of RidA chaperone function by N-chlorination

Alexandra Müller, Sina Langklotz, Nataliya Lupilova, Katja Kuhlmann, Julia Elisabeth Bandow and Lars Ingo Ole Leichert ()
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Alexandra Müller: Institute of Biochemistry and Pathobiochemistry—Microbial Biochemistry, Ruhr-Universität Bochum
Sina Langklotz: Biology of Microorganisms, Ruhr-Universität Bochum
Nataliya Lupilova: Institute of Biochemistry and Pathobiochemistry—Microbial Biochemistry, Ruhr-Universität Bochum
Katja Kuhlmann: Medizinisches Proteom-Center, Ruhr-Universität Bochum
Julia Elisabeth Bandow: Biology of Microorganisms, Ruhr-Universität Bochum
Lars Ingo Ole Leichert: Institute of Biochemistry and Pathobiochemistry—Microbial Biochemistry, Ruhr-Universität Bochum

Nature Communications, 2014, vol. 5, issue 1, 1-14

Abstract: Abstract Escherichia coli RidA is a member of a structurally conserved, yet functionally highly diverse protein family involved in translation inhibition (human), Hsp90-like chaperone activity (fruit fly) and enamine/imine deamination (Salmonella enterica). Here, we show that E. coli RidA modified with HOCl acts as a highly effective chaperone. Although activation of RidA is reversed by treatment with DTT, ascorbic acid, the thioredoxin system and glutathione, it is independent of cysteine modification. Instead, treatment with HOCl or chloramines decreases the amino group content of RidA by reversibly N-chlorinating positively charged residues. N-chlorination increases hydrophobicity of RidA and promotes binding to a wide spectrum of unfolded cytosolic proteins. Deletion of ridA results in an HOCl-sensitive phenotype. HOCl-mediated N-chlorination thus is a cysteine-independent post-translational modification that reversibly turns RidA into an effective chaperone holdase, which plays a crucial role in the protection of cytosolic proteins during oxidative stress.

Date: 2014
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DOI: 10.1038/ncomms6804

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