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Bacillus subtilis ClpP degradome

ABSTRACT: To characterize the proteins substrates and the modifications of the ClpP protease of Bacillus subtilis.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Bacillus Subtilis Subsp. Subtilis Str. 168

TISSUE(S): Prokaryotic Cell

SUBMITTER: Debora Broch Trentini

LAB HEAD: Karl Mechtler

PROVIDER: PXD003305 | Pride | 2016-10-10

REPOSITORIES: Pride

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Arginine phosphorylation marks proteins for degradation by a Clp protease.

Trentini Débora Broch DB Suskiewicz Marcin Józef MJ Heuck Alexander A Kurzbauer Robert R Deszcz Luiza L Mechtler Karl K Clausen Tim T

Nature 20161006 7627

Protein turnover is a tightly controlled process that is crucial for the removal of aberrant polypeptides and for cellular signalling. Whereas ubiquitin marks eukaryotic proteins for proteasomal degradation, a general tagging system for the equivalent bacterial Clp proteases is not known. Here we describe the targeting mechanism of the ClpC-ClpP proteolytic complex from Bacillus subtilis. Quantitative affinity proteomics using a ClpP-trapping mutant show that proteins phosphorylated on arginine ...[more]

PMID: 27749819

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