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Isolation and identification of a fourth subunit in the membrane part of the chloroplast ATP‐synthase
Author(s) -
Fromme Petra,
Gräber Peter,
Salnikow Johann
Publication year - 1987
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 - 10.1016/0014-5793(87)81011-6
Subject(s) - protein subunit , chloroplast , atp synthase , biochemistry , molecular mass , gel electrophoresis , microbiology and biotechnology , coomassie brilliant blue , biology , polyacrylamide gel electrophoresis , peptide sequence , amino acid , chemistry , gene , enzyme , genetics , staining
The subunit composition of highly active purified ATP‐synthase from chloroplasts, CF 0 F 1 , was investigated by SDS gel electrophoresis. An additional subunit of CF 0 , was detected with an apparent molecular mass of 20 kDa. It is stained weakly with Coomassie blue but very strongly with silver. This subunit was isolated on a preparative SDS gel and the N‐terminal amino acid sequence analyzed. It shows that the 20 kDa protein is identical with the protein encoded by the spinach chloroplast gene atp I, called subunit IV [(1986) Mol. Genet. 203, 117–128]. However, in comparison to the gene‐derived sequence, the first 18 amino acids are missing, indicating N‐terminal processing.