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The transit peptide of CP29 thylakoid protein in Chlamydomonas reinhardtii is not removed but undergoes acetylation and phosphorylation
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
2004 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 564, no 1-2, 104-108 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
Amsterdam: Elsevier, 2004. Vol. 564, no 1-2, 104-108 p.
Keyword [en]
Transit peptide, Thylakoid membrane, CP29, Protein phosphorylation, Mass spectrometry, Chlamydomonas reinhardtii
National Category
Cell Biology Biochemistry and Molecular Biology Biophysics
URN: urn:nbn:se:umu:diva-18870DOI: 10.1016/S0014-5793(04)00323-0ISI: 000221032000017PubMedID: 15094049OAI: diva2:175001
Available from: 2009-02-26 Created: 2009-02-26 Last updated: 2016-08-11Bibliographically approved

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Villarejo, Arsenio
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Department of Plant PhysiologyUmeå Plant Science Centre (UPSC)
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ReferencesLink to record
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