IMMUNOCHEMICAL STUDIES ON THE CLP-PROTEASE IN CHLOROPLASTS - EVIDENCEFOR THE FORMATION OF A CLPC P COMPLEX/

Citation
M. Desimone et al., IMMUNOCHEMICAL STUDIES ON THE CLP-PROTEASE IN CHLOROPLASTS - EVIDENCEFOR THE FORMATION OF A CLPC P COMPLEX/, Botanica acta, 110(3), 1997, pp. 234-239
Citations number
34
Categorie Soggetti
Plant Sciences
Journal title
ISSN journal
09328629
Volume
110
Issue
3
Year of publication
1997
Pages
234 - 239
Database
ISI
SICI code
0932-8629(1997)110:3<234:ISOTCI>2.0.ZU;2-F
Abstract
Chloroplasts contain a proteolytic system whose activity is ATP-depend ent. The presence of genes encoding homologues of the ATP-dependent E. coli ClpA/P protease on the plastome and nuclear genome suggests that a similar protease is located in chloroplasts. Antibodies raised again st a recombinant chloroplast-encoded proteolytic ClpP subunit detect t his polypeptide in chloroplasts prepared from barley leaves or the euk aryotic algae Chlamydomonos reinhardtii and Eugleno gracitis. Co-immun oprecipitation experiments using the anti-ClpP antibody and an antibod y against the nuclear encoded regulatory ClpC component (a ClpA homolo gue) provide direct evidence for the existence of a ClpC/P complex in the chloroplast stroma. These results suggest that at least a part of the ATP-dependent proteolytic reactions in the chloroplast is catalyze d by an enzyme complex similar to the E.coli ClpA/P protease.