Proteomics

Dataset Information

0

Bacillus subtilis ClpP degradome

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

INSTRUMENT(S):

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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Dataset's files

Source:
Action DRS
20140908_Velos1_RSLC2_Broch_Trentini_Clausen_IMP_shotgun_Bsub_deltaClpC_37oCTiO2_4.msf Msf
20140908_Velos1_RSLC2_Broch_Trentini_Clausen_IMP_shotgun_Bsub_deltaClpC_37oCTiO2_4.raw Raw
20140908_Velos1_RSLC2_Broch_Trentini_Clausen_IMP_shotgun_Bsub_deltaClpC_45oC_TiO2_4-01.msf Msf
20140908_Velos1_RSLC2_Broch_Trentini_Clausen_IMP_shotgun_Bsub_deltaClpC_45oC_TiO2_4.raw Raw
20141117_Velos1_RSLC2_BrochTrentini_Clausen_IMP_insol_ClpP_TRAP_XM_pulldown1_try_rep1.raw Raw
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Publications

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]