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The transit peptide of CP29 thylakoid protein in Chlamydomonas reinhardtii is not removed but undergoes acetylation and phosphorylation
Author(s) -
Turkina Maria V,
Villarejo Arsenio,
Vener Alexander V
Publication year - 2004
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(04)00323-0
Subject(s) - chlamydomonas reinhardtii , thylakoid , transit peptide , chlamydomonas , phosphorylation , biochemistry , peptide , acetylation , chemistry , photosystem ii , threonine , protein phosphorylation , biology , serine , chloroplast , photosynthesis , mutant , gene , protein kinase a , plastid
The surface‐exposed peptides were cleaved by trypsin from the photosynthetic thylakoid membranes isolated from the green alga Chlamydomonas reinhardtii . Two phosphorylated peptides, enriched from the peptide mixture and sequenced by nanospray quadrupole time‐of‐flight mass spectrometry, revealed overlapping sequences corresponding to the N‐terminus of a nuclear‐encoded chlorophyll a / b ‐binding protein CP29. In contrast to all known nuclear‐encoded thylakoid proteins, the transit peptide in the mature algal CP29 was not removed but processed by methionine excision, N‐terminal acetylation and phosphorylation on threonine 6. The importance of this phosphorylation site is proposed as the reason of the unique transit peptide retention.