Arginine phosphorylation marks proteins for degradation by a Clp protease

Débora Broch Trentini, Marcin Józef Suskiewicz, Alexander Heuck, Robert Kurzbauer, Luiza Deszcz, Karl Mechtler and Tim Clausen ()
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Débora Broch Trentini: Research Institute of Molecular Pathology (IMP), Dr-Bohr-Gasse 7
Marcin Józef Suskiewicz: Research Institute of Molecular Pathology (IMP), Dr-Bohr-Gasse 7
Alexander Heuck: Research Institute of Molecular Pathology (IMP), Dr-Bohr-Gasse 7
Robert Kurzbauer: Research Institute of Molecular Pathology (IMP), Dr-Bohr-Gasse 7
Luiza Deszcz: Research Institute of Molecular Pathology (IMP), Dr-Bohr-Gasse 7
Karl Mechtler: Research Institute of Molecular Pathology (IMP), Dr-Bohr-Gasse 7
Tim Clausen: Research Institute of Molecular Pathology (IMP), Dr-Bohr-Gasse 7

Nature, 2016, vol. 539, issue 7627, 48-53

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

Date: 2016
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DOI: 10.1038/nature20122

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