title: N- and O-acetylation of threonine residues in the context of proteomics.
abstract: The detection of post-translational modifications (PTMs) of proteins is a matter of intensive research. Among all possible pitfalls that may lead to misidentifications, the chemical stability of modified peptides is scarcely questioned. Global proteomic studies devoted to protein acetylation are becoming popular. Thus, we were concerned about the intrinsic stability of O-acetylated peptides because of the O-N acyl transfer reactivity occurring when an amino moiety is present in the vicinity of the acylated hydroxyl group. Here, the behavior of isomeric O- and N-acetylated, N-terminal threonine-containing peptides was explored in a standard proteomic workflow. We demonstrated a strong chemical instability of O-acetylation, which prevents its detection.
authors.affiliation: CEA, DSV, IBEB, Lab Biochim System Perturb, Bagnols-sur-Cèze F-30207, France.
authors.forename: Jean-Baptiste
authors.initials: JB
authors.lastname: Boyer
authors.affiliation: CEA, DSV, IBEB, Lab Biochim System Perturb, Bagnols-sur-Cèze F-30207, France.
authors.forename: Alain
authors.initials: A
authors.lastname: Dedieu
authors.affiliation: CEA, DSV, IBEB, Lab Biochim System Perturb, Bagnols-sur-Cèze F-30207, France.
authors.forename: Jean
authors.initials: J
authors.lastname: Armengaud
authors.affiliation: Institut des Biomolécules Max Mousseron (IBMM), UMR 5247, Universités Montpellier 1 et 2, CNRS, Bâtiment Chimie (17), Université Montpellier 2, Place Eugène Bataillon, 34095 Montpellier Cedex 5, France.
authors.forename: Pascal
authors.initials: P
authors.lastname: Verdié
authors.affiliation: Institut des Biomolécules Max Mousseron (IBMM), UMR 5247, Universités Montpellier 1 et 2, CNRS, Bâtiment Chimie (17), Université Montpellier 2, Place Eugène Bataillon, 34095 Montpellier Cedex 5, France.
authors.forename: Gilles
authors.initials: G
authors.lastname: Subra
authors.affiliation: Institut des Biomolécules Max Mousseron (IBMM), UMR 5247, Universités Montpellier 1 et 2, CNRS, Bâtiment Chimie (17), Université Montpellier 2, Place Eugène Bataillon, 34095 Montpellier Cedex 5, France.
authors.forename: Jean
authors.initials: J
authors.lastname: Martinez
authors.affiliation: Institut des Biomolécules Max Mousseron (IBMM), UMR 5247, Universités Montpellier 1 et 2, CNRS, Bâtiment Chimie (17), Université Montpellier 2, Place Eugène Bataillon, 34095 Montpellier Cedex 5, France. Electronic address: enjalbal@univ-montp2.fr.
authors.forename: Christine
authors.initials: C
authors.lastname: Enjalbal
mesh_terms: D000107:Acetylation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D013912:Threonine / Q000032:analysis / Q000737:chemistry*
chemical_list: D011506:Proteins; D013912:Threonine
keywords: O-acetyl threonine; O–N acetyl transfer; O–N acyl shift; Protein post-translational acetylation; Threonine acetylation