title: Protein N-terminal methionine excision.
abstract: N-terminal methionine excision (NME) is the major proteolytic pathway responsible for the diversity of N-terminal amino acids in proteins. Dedicated NME components have been identified in all organisms, in all compartments in which protein synthesis occurs: cytoplasm, plastids and mitochondria. Recent studies have revealed that NME is regulated at various levels and plays an important role in controlling protein turnover. NME is essential in Eubacteria and lower eukaryotes and is the target of many natural and synthetic inhibitors. Such inhibitors have considerable potential for use in the treatment of various human diseases, from cancer to bacterial and parasitic infections.
authors.affiliation: Protein Maturation Group, Institut des Sciences du Végétal, UPR2355, Centre National de la Recherche Scientifique, Bâtiment 23, 1 avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
authors.forename: C
authors.initials: C
authors.lastname: Giglione
authors.forename: A
authors.initials: A
authors.lastname: Boularot
authors.forename: T
authors.initials: T
authors.lastname: Meinnel
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry*; D000626:Aminopeptidases / Q000737:chemistry; D000818:Animals; D002412:Cations; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D006801:Humans; D045726:Metalloproteases / Q000378:metabolism; D008715:Methionine / Q000737:chemistry*; D008928:Mitochondria / Q000378:metabolism; D008956:Models, Chemical; D010802:Phylogeny; D018087:Plastids / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D020543:Proteome / Q000737:chemistry
chemical_list: D002412:Cations; D011506:Proteins; D020543:Proteome; D008715:Methionine; D045726:Metalloproteases; D000626:Aminopeptidases; D000581:Amidohydrolases; C084507:peptide deformylase