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Characterization of ClpS2, an essential adaptor protein for the cyanobacterium Synechococcus elongatus

Journal article
Authors Anders Tryggvesson
Frida Ståhlberg
Mats H. Töpel
Noriaki Tanabe
A. Mogk
Adrian K Clarke
Published in Febs Letters
Volume 589
Issue 24
Pages 4039-4046
ISSN 0014-5793
Publication year 2015
Published at Department of Biological and Environmental Sciences
Pages 4039-4046
Language en
Links dx.doi.org/10.1016/j.febslet.2015.1...
Keywords N-end rule, ClpS adaptor, Proteolysis, Synechococcus elongatus, n-end rule, escherichia-coli, molecular-basis, pcc 7942, degradation, substrate, clpap, chaperone, pathway, recognition, Biochemistry & Molecular Biology, Biophysics, Cell Biology
Subject categories Biochemistry and Molecular Biology, Biophysics, Cell Biology

Abstract

The adaptor protein ClpS associates to the Clp protease and promotes degradation of N-end rule substrates in eubacteria and in algal/plant chloroplasts. Cyanobacteria are unusual in having two distinct ClpS paralogs. Although ClpS1 is typical of bacterial ClpS, ClpS2 differs in crucial ways. ClpS2 in Synechococcus elongatus is a relatively low- abundant, soluble protein essential for phototrophic growth. Like ClpS1, ClpS2 binds to the ClpCP3/R protease to block alpha-casein degradation and promote that of N-end rule substrates in vitro. However, their substrate specificity differs, with ClpS1 recognizing destabilizing Phe and Tyr residues at the substrate N-terminus whereas ClpS2 recognizes Leu. Overall, ClpS2 appears to have independently evolved in cyanobacteria to degrade a particular group of proteins, whose turnover is vital for cell viability. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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