期刊
FEBS LETTERS
卷 564, 期 1-2, 页码 104-108出版社
WILEY
DOI: 10.1016/S0014-5793(04)00323-0
关键词
transit peptide; thylakoid membrane; CP29; protein phosphorylation; mass spectrometry; Chlamydomonas reinhardtii
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. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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