Purification properties and biogenesis of Chlamydomonas reinhardii photosystem I reaction center.

R. Nechushtai*, N. Nelson

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

62 Scopus citations

Abstract

A photosystem I reaction center was isolated from Chlamydomonas reinhardii chloroplasts. It consists of four different polypeptides with Mr approximately 70,000 (subunit I), 19,000 (subunit II), 10,000 (subunit III), and 8,000 (subunit IV). In the presence of salts, the purified reaction center was active in cytochrome 552 photooxidation. Short term labeling experiments with [35S]sulfate revealed that subunit III contains no cysteine or methionine. Subunits I and IV were shown to be chloroplast translation products, while subunit II appears to be synthesized on cytoplasmic ribosomes. The site of synthesis of the subunits to the proton-ATPase complex was studied. A differential effect of cycloheximide on the assembly of photosystem I reaction center and the proton-ATPase complex was indicated.

Original languageAmerican English
Pages (from-to)11624-11628
Number of pages5
JournalJournal of Biological Chemistry
Volume256
Issue number22
StatePublished - 25 Nov 1981

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