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Article Dans Une Revue EMBO Journal Année : 2003

Control of protein life-span by N-terminal methionine excision.

Résumé

Peptide deformylases (PDFs) have been discovered recently in eukaryotic genomes, and it appears that N-terminal methionine excision (NME) is a conserved pathway in all compartments where protein synthesis occurs. This work aimed at uncovering the function(s) of NME in a whole proteome, using the chloroplast-encoded proteins of both Arabidopsis thaliana and Chlamydomonas reinhardtii as model systems. Disruption of PDF1B in A.thaliana led to an albino phenotype, and an extreme sensitivity to the PDF- specific inhibitor actinonin. In contrast, a knockout line for PDF1A exhibited no apparent phenotype. Photosystem II activity in C.reinhardtii cells was substantially reduced by the presence of actinonin. Pulse-chase experiments revealed that PDF inhibition leads to destabilization of a crucial subset of chloroplast-encoded photosystem II components in C. reinhardtii. The same proteins were destabilized in pdf1b. Site-directed substitutions altering NME of the most sensitive target, subunit D2, resulted in similar effects. Thus, plastid NME is a critical mechanism specifically influencing the life-span of photosystem II polypeptides. A general role of NME in modulating the half-life of key subsets of proteins is suggested.

Dates et versions

hal-00135717 , version 1 (08-03-2007)

Identifiants

Citer

Carmela Giglione, Olivier Vallon, Thierry Meinnel. Control of protein life-span by N-terminal methionine excision.. EMBO Journal, 2003, 22 (1), pp.13-23. ⟨10.1093/emboj/cdg007⟩. ⟨hal-00135717⟩
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