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Effect of precursor protein phosphorylation on import into isolated chloroplasts from Chlamydomonas
Author(s) -
Su Qingxiang,
Schmid Katharina,
Schild Christof,
Boschetti Arminio
Publication year - 2001
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/s0014-5793(01)03012-5
Subject(s) - chlamydomonas reinhardtii , chlamydomonas , chloroplast , phosphorylation , transit peptide , protein phosphorylation , protein subunit , biochemistry , rubisco , biology , microbiology and biotechnology , protein kinase a , photosynthesis , gene , plastid , mutant
In higher plants, chloroplast‐destined precursor proteins are thought to be phosphorylated. Mediated by a specific 14‐3‐3 protein, these phosphorylated proteins bind to the chloroplast surface and are subsequently imported into the chloroplast. We demonstrate that also in the green alga Chlamydomonas reinhardtii the precursor of the small subunit of ribulose‐1,5‐bisphosphate carboxylase becomes phosphorylated by a plant protein kinase and that the phosphorylation site is located in the transit peptide. The phosphorylation status of the precursor protein regulates its import into chloroplasts especially at an early step during this process. The possible physiological function is discussed.