The alpha-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in gamma-proteobacteria

Walden, Patricia, Halili, Maria, Julia Archbold, Fredrik Lindahl, Fairlie, David P., Inaba, Kenji and Martin, Jennifer L. (2013) The alpha-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in gamma-proteobacteria. PloS One, 8 11: e81440.1-e81440.9. doi:10.1371/journal.pone.0081440


Author Walden, Patricia
Halili, Maria
Julia Archbold
Fredrik Lindahl
Fairlie, David P.
Inaba, Kenji
Martin, Jennifer L.
Title The alpha-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in gamma-proteobacteria
Formatted title
The α-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in γ-proteobacteria
Journal name PloS One   Check publisher's open access policy
ISSN 1932-6203
Publication date 2013-11-25
Sub-type Article (original research)
DOI 10.1371/journal.pone.0081440
Open Access Status DOI
Volume 8
Issue 11
Start page e81440.1
End page e81440.9
Total pages 9
Editor Emily Parker
Place of publication San Francisco, CA, United States
Publisher Public Library of Science
Collection year 2014
Language eng
Formatted abstract
The α-proteobacterium Wolbachia pipientis infects more than 65% of insect species worldwide and manipulates the host reproductive machinery to enable its own survival. It can live in mutualistic relationships with hosts that cause human disease, including mosquitoes that carry the Dengue virus. Like many other bacteria, Wolbachia contains disulfide bond forming (Dsb) proteins that introduce disulfide bonds into secreted effector proteins. The genome of the Wolbachia strain wMel encodes two DsbA-like proteins sharing just 21% sequence identity to each other, α-DsbA1 and α-DsbA2, and an integral membrane protein, α-DsbB. α-DsbA1 and α-DsbA2 both have a Cys-X-X-Cys active site that, by analogy with Escherichia coli DsbA, would need to be oxidized to the disulfide form to serve as a disulfide bond donor toward substrate proteins. Here we show that the integral membrane protein α-DsbB oxidizes α-DsbA1, but not α-DsbA2. The interaction between α-DsbA1 and α-DsbB is very specific, involving four essential cysteines located in the two periplasmic loops of α-DsbB. In the electron flow cascade, oxidation of α-DsbA1 by α-DsbB is initiated by an oxidizing quinone cofactor that interacts with the cysteine pair in the first periplasmic loop. Oxidizing power is transferred to the second cysteine pair, which directly interacts with α-DsbA1. This reaction is inhibited by a non-catalytic disulfide present in α-DsbA1, conserved in other α-proteobacterial DsbAs but not in γ-proteobacterial DsbAs. This is the first characterization of the integral membrane protein α-DsbB from Wolbachia and reveals that the non-catalytic cysteines of α-DsbA1 regulate the redox relay system in cooperation with α-DsbB.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
Institute for Molecular Bioscience - Publications
 
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Created: Tue, 10 Dec 2013, 11:40:41 EST by Susan Allen on behalf of Institute for Molecular Bioscience