title: N-terminal protein modifications: Bringing back into play the ribosome.
abstract: N-terminal protein modifications correspond to the first modifications which in principle any protein may undergo, before translation is completed by the ribosome. This class of essential modifications can have different nature or function and be catalyzed by a variety of dedicated enzymes. Here, we review the current state of the major N-terminal co-translational modifications, with a particular emphasis to their catalysts, which belong to metalloprotease and acyltransferase clans. The earliest of these modifications corresponds to the N-terminal methionine excision, an ubiquitous and essential process leading to the removal of the first methionine. N-alpha acetylation occurs also in all Kingdoms although its extent appears to be significantly increased in higher eukaryotes. Finally, N-myristoylation is a crucial pathway existing only in eukaryotes. Recent studies dealing on how some of these co-translational modifiers might work in close vicinity of the ribosome is starting to provide new information on when these modifications exactly take place on the elongating nascent chain and the interplay with other ribosome biogenesis factors taking in charge the nascent chains. Here a comprehensive overview of the recent advances in the field of N-terminal protein modifications is given.
authors.affiliation: CNRS, Institut des Sciences du Végétal, 1 Avenue de la Terrasse, Bât 23A, F-91198 Gif sur Yvette, France; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, 1 Avenue de la Terrasse, 91198 Gif-sur-Yvette cedex, France. Electronic address: Carmela.Giglione@isv.cnrs-gif.fr.
authors.forename: Carmela
authors.initials: C
authors.lastname: Giglione
authors.affiliation: CNRS, Institut des Sciences du Végétal, 1 Avenue de la Terrasse, Bât 23A, F-91198 Gif sur Yvette, France; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, 1 Avenue de la Terrasse, 91198 Gif-sur-Yvette cedex, France.
authors.forename: Sonia
authors.initials: S
authors.lastname: Fieulaine
authors.affiliation: CNRS, Institut des Sciences du Végétal, 1 Avenue de la Terrasse, Bât 23A, F-91198 Gif sur Yvette, France; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, 1 Avenue de la Terrasse, 91198 Gif-sur-Yvette cedex, France. Electronic address: Thierry.Meinnel@isv.cnrs-gif.fr.
authors.forename: Thierry
authors.initials: T
authors.lastname: Meinnel
mesh_terms: D000581:Amidohydrolases / Q000502:physiology; D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D063208:Methionyl Aminopeptidases / Q000502:physiology; D008969:Molecular Sequence Data; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D012270:Ribosomes
chemical_list: D063208:Methionyl Aminopeptidases; D000581:Amidohydrolases; C084507:peptide deformylase
keywords: Co-translational modifications; Methionine aminopeptidase; N-myristoyltransferase; N-terminal; N-α-acetyltransferase; Peptide deformylase