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
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.