ZraP is a periplasmic molecular chaperone and a repressor of the zinc-responsive two-component regulator ZraSR

Appia‑Ayme, Corinne, Hall, Andrea, Patrick, Elaine, Rajadurai, Shiny, Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914 and Rowley, Gary (2012) ZraP is a periplasmic molecular chaperone and a repressor of the zinc-responsive two-component regulator ZraSR. Biochemical Journal, 442 (1). pp. 85-93. ISSN 0264-6021

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The bacterial envelope is the interface with the surrounding environment and is consequently subjected to a barrage of noxious agents including a range of compounds with antimicrobial activity. The ESR (envelope stress response) pathways of enteric bacteria are critical for maintenance of the envelope against these antimicrobial agents. In the present study, we demonstrate that the periplasmic protein ZraP contributes to envelope homoeostasis and assign both chaperone and regulatory function to ZraP from Salmonella Typhimurium. The ZraP chaperone mechanism is catalytic and independent of ATP; the chaperone activity is dependent on the presence of zinc, which is shown to be responsible for the stabilization of an oligomeric ZraP complex. Furthermore, ZraP can act to repress the two-component regulatory system ZraSR, which itself is responsive to zinc concentrations. Through structural homology, ZraP is a member of the bacterial CpxP family of periplasmic proteins, which also consists of CpxP and Spy. We demonstrate environmental co-expression of the CpxP family and identify an important role for these proteins in Salmonella's defence against the cationic antimicrobial peptide polymyxin B.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
UEA Research Groups: Faculty of Science > Research Groups > Molecular Microbiology
Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Faculty of Science > Research Groups > Energy Materials Laboratory
Depositing User: Users 2731 not found.
Date Deposited: 07 Feb 2012 14:27
Last Modified: 21 Dec 2022 16:31
URI: https://ueaeprints.uea.ac.uk/id/eprint/36899
DOI: 10.1042/BJ20111639


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