The transit peptide of CP29 thylakoid protein in Chlamydomonas reinhardtii is not removed but undergoes acetylation and phosphorylation. Turkina, M. V., Villarejo, A., & Vener, A. V. FEBS Letters, 564(1-2):104–108, 2004. _eprint: https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2804%2900323-0![The transit peptide of CP29 thylakoid protein in Chlamydomonas reinhardtii is not removed but undergoes acetylation and phosphorylation [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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.
@article{turkina_transit_2004,
title = {The transit peptide of {CP29} thylakoid protein in {Chlamydomonas} reinhardtii is not removed but undergoes acetylation and phosphorylation},
volume = {564},
issn = {1873-3468},
url = {https://febs.onlinelibrary.wiley.com/doi/abs/10.1016/S0014-5793%2804%2900323-0},
doi = {10.1016/S0014-5793(04)00323-0},
abstract = {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.},
language = {en},
number = {1-2},
urldate = {2021-06-30},
journal = {FEBS Letters},
author = {Turkina, Maria V. and Villarejo, Arsenio and Vener, Alexander V.},
year = {2004},
note = {\_eprint: https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793\%2804\%2900323-0},
keywords = {CID, CP29, Chlamydomonas reinhardtii, IMAC, LHCP, Mass spectrometry, Protein phosphorylation, Thylakoid membrane, Transit peptide, collision-induced dissociation, immobilized metal affinity chromatography, light-harvesting chlorophyll a/b-binding protein, minor chlorophyll a/b-binding protein of photosystem II},
pages = {104--108},
}
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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. 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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.},\n\tlanguage = {en},\n\tnumber = {1-2},\n\turldate = {2021-06-30},\n\tjournal = {FEBS Letters},\n\tauthor = {Turkina, Maria V. and Villarejo, Arsenio and Vener, Alexander V.},\n\tyear = {2004},\n\tnote = {\\_eprint: https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793\\%2804\\%2900323-0},\n\tkeywords = {CID, CP29, Chlamydomonas reinhardtii, IMAC, LHCP, Mass spectrometry, Protein phosphorylation, Thylakoid membrane, Transit peptide, collision-induced dissociation, immobilized metal affinity chromatography, light-harvesting chlorophyll a/b-binding protein, minor chlorophyll a/b-binding protein of photosystem II},\n\tpages = {104--108},\n}\n\n\n\n\n\n\n\n","author_short":["Turkina, M. V.","Villarejo, A.","Vener, A. 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