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FixK 2 , a key regulator in Bradyrhizobium japonicum , is a substrate for the protease ClpAP in vitro
Author(s) -
Bonnet Mariette,
Stegmann Monika,
Maglica Željka,
Stiegeler Emanuel,
Weber-Ban Eilika,
Hennecke Hauke,
Mesa Socorro
Publication year - 2013
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.2012.11.014
Subject(s) - protease , bradyrhizobium japonicum , proteases , regulator , proteolysis , biology , signal transducing adaptor protein , biochemistry , chemistry , microbiology and biotechnology , enzyme , signal transduction , rhizobiaceae , bacteria , genetics , symbiosis , gene
FixK 2 is a CRP‐like transcription factor that controls the endosymbiotic lifestyle of Bradyrhizobium japonicum . The reason for its noticeable protease sensitivity was explored here. The repertoire of Clp chaperone‐proteases in B. japonicum was examined, and specifically ClpAP 1 and ClpXP 1 were purified and tested. FixK 2 was found to be degraded by ClpAP 1 but not by ClpXP 1 . Degradation was inhibited by the ClpS 1 adaptor protein, indicating that FixK 2 is a direct substrate for ClpAP 1 . The last 12 amino acids of FixK 2 appeared to be recognized by ClpA. The results suggest that the ClpAP system is involved in the cellular turnover of FixK 2 .