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Characterization of ClpS2, an essential adaptor protein for the cyanobacterium Synechococcus elongatus
Author(s) -
Tryggvesson Anders,
Ståhlberg Frida M.,
Töpel Mats,
Tanabe Noriaki,
Mogk Axel,
Clarke Adrian K.
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.11.026
Subject(s) - cyanobacteria , synechococcus , protease , signal transducing adaptor protein , biochemistry , proteolysis , biology , chloroplast , protein degradation , chemistry , bacteria , microbiology and biotechnology , signal transduction , enzyme , gene , genetics
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 ClpSl 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 ClpSl, ClpS2 binds to the ClpCP3/R protease to block α‐casein degradation and promote that of N‐end rule substrates in vitro . However, their substrate specificity differs, with ClpSl 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.