PXD002804-1

PXD002804 is an original dataset announced via ProteomeXchange.

Title	Repairing oxidatively damaged proteins using electrons from the respiratory chain
Description	The reactive species of oxygen (ROS) and chlorine (RCS) damage cellular components, potentially leading to cell death. In proteins, the sulfur-containing amino acid methionine (Met) is converted to methionine sulfoxide (Met-O), which can cause a loss of biological activity. Here, we report the identification of an enzymatic system repairing proteins with oxidatively-damaged Met residues in the bacterial cell envelope, a compartment particularly exposed to the ROS and RCS generated by the host defense mechanisms. This system is made of the molybdenum-containing enzyme MsrP and the heme-binding membrane protein MsrQ. Both proteins, whose synthesis is induced by hypochlorous acid (HOCl), a powerful antimicrobial released by neutrophils, are widely conserved throughout Gram-negative bacteria, including major human pathogens. MsrPQ is essential for extracytosolic protein quality control and the maintenance of envelope integrity under bleach stress, rescuing Met residues from oxidation in a wide series of structurally unrelated periplasmic proteins. For this activity, MsrPQ uses electrons from the respiratory chain, which represents a novel mechanism to import reducing equivalents into the bacterial cell envelope. A remarkable feature of MsrPQ is its capacity to reduce both R- and S- diastereoisomers of Met-O, making this oxidoreductase complex functionally different from conventional methionine sulfoxide reductases (Msr). The surprising observation that the bacterial periplasm contains a single enzymatic complex able to fully protect Met residues from oxidative damage suggests that potentially similar systems exist in the endoplasmic reticulum (ER) and other subcellular oxidizing compartments
HostingRepository	PRIDE
AnnounceDate	2015-09-16
AnnouncementXML	Submission_2015-09-16_05:40:40.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Didier Vertommen
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	N-ethylmaleimide derivatized cysteine; monohydroxylated residue
Instrument	LTQ

Revision	Datetime	Status	ChangeLog Entry
0	2015-08-27 02:34:52	ID requested
⏵ 1	2015-09-16 05:40:41	announced
2	2015-09-18 00:32:28	announced	Updated project metadata.
3	2016-03-31 02:08:44	announced	Updated project metadata.

Dataset with its publication pending

submitter keyword: E. Coli, methione, ROS, repair

Jean-François Collet
contact affiliation	UCL - de Duve Institute Brussels Belgium
contact email	jfcollet@uclouvain.be
lab head
Didier Vertommen
contact affiliation	UCL - de Duve Institute, Brussels Belgium
contact email	didier.vertommen@uclouvain.be
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD002804
     1. Label: PRIDE project
     2. Name: Repairing oxidatively damaged proteins using electrons from the respiratory chain