Chloroplast-encoded protein as a subunit of acetyl-CoA carboxylase in pea plant.
The gene product of an open reading frame of the chloroplast genome, accD, that has sequence similarity with a subunit of acetyl-CoA carboxylase from Escherichia coli was detected immunochemically in pea chloroplasts. The apparent molecular mass of the accD protein was 87 kDa on SDS-polyacrylamide gel electrophoresis. The protein was acidic and had less mobility than the calculated value, 67,116. Acetyl-CoA carboxylase activity solubilized from pea chloroplasts was inhibited by antibodies against recombinant accD protein. The antibodies precipitated a polypeptide of 35 kDa containing biotin and a polypeptide of 91 kDa together with the 87-kDa-accD protein. The accD protein formed a complex with the molecular mass of about 700 kDa, probably with the 35- and 91-kDa proteins. These results indicate that the chloroplast-encoded polypeptide, accD protein, is a component of a functional acetyl-CoA carboxylase in chloroplasts and this enzyme is a multi-subunit complex, like that from E. coli. The synthesis of accD protein was not induced by light.
Sasaki
Y
Y
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.
Hakamada
K
K
Suama
Y
Y
Nagano
Y
Y
Furusawa
I
I
Matsuno
R
R
D000103:Acetyl-CoA Carboxylase / Q000235:genetics*; D001483:Base Sequence; D002736:Chloroplasts / Q000378:metabolism*; D017931:DNA Primers; D007887:Fabaceae / Q000201:enzymology* / Q000235:genetics / Q000648:ultrastructure; D007120:Immunochemistry; D008027:Light; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000235:genetics*; D010946:Plants, Medicinal
D017931:DNA Primers; D010940:Plant Proteins; D000103:Acetyl-CoA Carboxylase