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Immunochemical Studies on the Clp‐protease in Chloroplasts: Evidence for the Formation of a CIpC/P Complex *
Author(s) -
Desimone M.,
WeißWichert C.,
Wagner E.,
Altenfeld Ursula,
Johanningmeier U.
Publication year - 1997
Publication title -
botanica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 0932-8629
DOI - 10.1111/j.1438-8677.1997.tb00634.x
Subject(s) - chlamydomonas reinhardtii , chloroplast , protease , chloroplast dna , biology , chlamydomonas , protein subunit , euglena , recombinant dna , biochemistry , microbiology and biotechnology , gene , enzyme , mutant
Chloroplasts contain a proteolytic system whose activity is ATP‐dependent. The presence of genes encoding homologues of the ATP‐dependent E. coli CIpA/P protease on the plastome and nuclear genome suggests that a similar protease is located in chloroplasts. Antibodies raised against a recombinant chloroplast‐encoded proteolytic ClpP subunit detect this polypeptide in chloroplasts prepared from barley leaves or the eukaryotic algae Chlamydomonas reinhardtii and Euglena gracilis . Co‐immunoprecipitation experiments using the anti‐ClpP antibody and an antibody against the nuclear encoded regulatory CIpC component (a ClpA homologue) provide direct evidence for the existence of a CIpC/P complex in the chloroplast stroma. These results suggest that at least a part of the ATP‐dependent proteolytic reactions in the chloroplast is catalyzed by an enzyme complex similar to the E. coli CIpA/P protease.