dc.contributor.author | Walden, Patricia M | |
dc.contributor.author | Halili, Maria A | |
dc.contributor.author | Archbold, Julia K | |
dc.contributor.author | Lindahl, Fredrik | |
dc.contributor.author | Fairlie, David P | |
dc.contributor.author | Inaba, Kenji | |
dc.contributor.author | Martin, Jennifer L | |
dc.date.accessioned | 2018-01-19T05:11:49Z | |
dc.date.available | 2018-01-19T05:11:49Z | |
dc.date.issued | 2013 | |
dc.identifier.issn | 1932-6203 | |
dc.identifier.doi | 10.1371/journal.pone.0081440 | |
dc.identifier.uri | http://hdl.handle.net/10072/171884 | |
dc.description.abstract | The a-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, a-DsbA1 and a-DsbA2, and an
integral membrane protein, a-DsbB. a-DsbA1 and a-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 a-DsbB oxidizes a-DsbA1, but not a-DsbA2. The interaction
between a-DsbA1 and a-DsbB is very specific, involving four essential cysteines located in the two periplasmic loops of a-
DsbB. In the electron flow cascade, oxidation of a-DsbA1 by a-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 a-DsbA1. This reaction is inhibited by a non-catalytic disulfide present in a-DsbA1, conserved in
other a-proteobacterial DsbAs but not in c-proteobacterial DsbAs. This is the first characterization of the integral membrane
protein a-DsbB from Wolbachia and reveals that the non-catalytic cysteines of a-DsbA1 regulate the redox relay system in
cooperation with a-DsbB. | |
dc.description.peerreviewed | Yes | |
dc.language | English | |
dc.language.iso | eng | |
dc.publisher | Public Library of Sciences | |
dc.relation.ispartofpagefrom | e81440-1 | |
dc.relation.ispartofpageto | e81440-9 | |
dc.relation.ispartofissue | 11 | |
dc.relation.ispartofjournal | PLoS One | |
dc.relation.ispartofvolume | 8 | |
dc.subject.fieldofresearch | Biochemistry and cell biology not elsewhere classified | |
dc.subject.fieldofresearchcode | 310199 | |
dc.title | The α-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in γ-proteobacteria | |
dc.type | Journal article | |
dc.type.description | C1 - Articles | |
dc.type.code | C - Journal Articles | |
dcterms.license | https://creativecommons.org/licenses/by/4.0/ | |
dc.description.version | Version of Record (VoR) | |
gro.rights.copyright | © 2013 Walden et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits
unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. | |
gro.hasfulltext | Full Text | |
gro.griffith.author | Martin, Jennifer | |