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Dynamics of post‐translational modifications and protein stability in the stroma of Chlamydomonas reinhardtii chloroplasts
Author(s) -
Bienvenut Willy V.,
Espagne Christelle,
Martinez Aude,
Majeran Wojetec,
Valot Benoît,
Zivy Michel,
Vallon Olivier,
Adam Zach,
Meinnel Thierry,
Giglione Carmela
Publication year - 2011
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201000634
Subject(s) - chlamydomonas reinhardtii , proteome , biology , chlamydomonas , chloroplast , in silico , acetylation , stromal cell , microbiology and biotechnology , biochemistry , computational biology , mutant , gene , cancer research
The proteome of any system is a dynamic entity dependent on the intracellular concentration of the entire set of expressed proteins. In turn, this whole protein concentration will be reliant on the stability/turnover of each protein as dictated by their relative rates of synthesis and degradation. In this study, we have investigated the dynamics of the stromal proteome in the model organism Chlamydomonas reinhardtii by characterizing the half-life of the whole set of proteins. 2-DE stromal proteins profiling was set up and coupled with MS analyses. These identifications featuring an average of 26% sequence coverage and eight non-redundant peptides per protein have been obtained for 600 independent samples related to 253 distinct spots. An interactive map of the global stromal proteome, of 274 distinct protein variants is now available on-line at http://www.isv.cnrs-gif.fr/gel2dv2/. N-α-terminal-Acetylation (NTA) was noticed to be the most frequently detectable post-translational modification, and new experimental data related to the chloroplastic transit peptide cleavage site was obtained. Using this data set supplemented with series of pulse-chase experiments, elements directing the relationship between half-life and N-termini were analyzed. Positive correlation between NTA and protein half-life suggests that NTA could contribute to protein stabilization in the stroma.