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Publication Abstract from PubMed

Protein turnover is a tightly controlled process critical 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 address 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 residues are selectively targeted to ClpC:ClpP. In vitro reconstitution experiments reveal that the McsB-mediated arginine phosphorylation is required and sufficient for the degradation of substrate proteins. The docking site for phosphoarginine is located in the N-terminal domain of the ClpC ATPase as resolved at high resolution in a co-crystal structure. Together, our data demonstrate that pArg functions as a bona fide degradation tag for the ClpC:ClpP protease. This system, widely distributed across Gram-positive bacteria, is functionally analogous to the eukaryotic ubiquitin-proteasome system.

Arginine phosphorylation marks proteins for degradation by a Clp protease.,Trentini DB, Suskiewicz MJ, Heuck A, Kurzbauer R, Deszcz L, Mechtler K, Clausen T Nature. 2016 Oct 6. doi: 10.1038/nature20122. PMID:27749819^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.