The transit peptide of CP29 thylakoid protein in Chlamydomonas reinhardtii is not removed but undergoes acetylation and phosphorylation

FEBS Letters

Turkina, Maria V¹  Vener, Alexander V¹  Villarejo, Arsenio² 

[1] Division of Cell Biology, University of Linköping, 581 85 Linköping, Sweden;Umeå Plant Science Center, Department of Plant Physiology, University of Umeå, 901 87 Umeå, Sweden

关键词: Transit peptide;    Thylakoid membrane;    CP29;    Protein phosphorylation;    Mass spectrometry;    Chlamydomonas reinhardtii;    CID;    collision-induced dissociation;    CP29;    minor chlorophyll a/b-binding protein of photosystem II;    IMAC;    immobilized metal affinity chromatography;    LHCP;    light-harvesting chlorophyll a/b-binding protein;   

DOI  :  10.1016/S0014-5793(04)00323-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown