Isolation and identification of a fourth subunit in the membrane part of the chloroplast ATP‐synthase

FEBS Letters

Fromme, Petra¹  Salnikow, Johann²  Gräber, Peter¹ 

[1] Max-Volmer-Institut für Biophysikalische und Physikalische Chemie, Technische Universität Berlin, Straße des 17 Juni 135, 1000 Berlin 12, Germany;Institut für Biochemie und Molekulare Biologie, Technische Universität Berlin, Franklinstr. 29, 1000 Berlin 10, Germany

关键词: Chloroplast;    ATP-synthase;    CF0F1;    CF0 subunit;    Amino acid sequence;    CF0F1;    proton translocating ATP-synthase from chloroplasts;    HPLC;    high-pressure liquid chromatography;   

DOI  :  10.1016/0014-5793(87)81011-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The subunit composition of highly active purified ATP-synthase from chloroplasts, CF₀F₁, was investigated by SDS gel electrophoresis. An additional subunit of CF₀, 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 atpI, 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.

【 授权许可】

Unknown