title: The Protein Acetyltransferase PatZ from Escherichia coli Is Regulated by Autoacetylation-induced Oligomerization.
abstract: Lysine acetylation is an important post-translational modification in the metabolic regulation of both prokaryotes and eukaryotes. In Escherichia coli, PatZ (formerly YfiQ) is the only known acetyltransferase protein and is responsible for acetyl-CoA synthetase acetylation. In this study, we demonstrated PatZ-positive cooperativity in response to acetyl-CoA and the regulation of acetyl-CoA synthetase activity by the acetylation level. Furthermore, functional analysis of an E809A mutant showed that the conserved glutamate residue is not relevant for the PatZ catalytic mechanism. Biophysical studies demonstrated that PatZ is a stable tetramer in solution and is transformed to its octameric form by autoacetylation. Moreover, this modification is reversed by the sirtuin CobB. Finally, an in silico PatZ tetramerization model based on hydrophobic and electrostatic interactions is proposed and validated by three-dimensional hydrodynamic analysis. These data reveal, for the first time, the structural regulation of an acetyltransferase by autoacetylation in a prokaryotic organism.
authors.affiliation: From the Departments of Biochemistry and Molecular Biology and Immunology (B) and tdp@um.es.
authors.forename: Teresa
authors.initials: T
authors.lastname: de Diego Puente
authors.affiliation: From the Departments of Biochemistry and Molecular Biology and Immunology (B) and.
authors.forename: Julia
authors.initials: J
authors.lastname: Gallego-Jara
authors.affiliation: From the Departments of Biochemistry and Molecular Biology and Immunology (B) and.
authors.forename: Sara
authors.initials: S
authors.lastname: Castaño-Cerezo
authors.affiliation: From the Departments of Biochemistry and Molecular Biology and Immunology (B) and.
authors.forename: Vicente
authors.initials: V
authors.lastname: Bernal Sánchez
authors.affiliation: Physical Chemistry, Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum," P. O. Box 4021, Murcia E-30100, Spain.
authors.forename: Vanesa
authors.initials: V
authors.lastname: Fernández Espín
authors.affiliation: Physical Chemistry, Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum," P. O. Box 4021, Murcia E-30100, Spain.
authors.forename: José
authors.initials: J
authors.lastname: García de la Torre
authors.affiliation: From the Departments of Biochemistry and Molecular Biology and Immunology (B) and.
authors.forename: Arturo
authors.initials: A
authors.lastname: Manjón Rubio
authors.affiliation: From the Departments of Biochemistry and Molecular Biology and Immunology (B) and.
authors.forename: Manuel
authors.initials: M
authors.lastname: Cánovas Díaz
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019943:Amino Acid Substitution; D000818:Animals; D003066:Coenzyme A Ligases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D020125:Mutation, Missense; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D037761:Sirtuins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; D000123:Acetyltransferases; C561243:acetyl-CoA synthetase acetylase, E coli; D037761:Sirtuins; C483998:cobB protein, E Coli; D003066:Coenzyme A Ligases; C101958:acetate-CoA ligase (ADP-forming)
keywords: Escherichia coli (E. coli); acetyl coenzyme A (acetyl-CoA); acetyl-CoA synthetase; acetyltransferase; autoacetylation; lysine acetylation; oligomerization; post-translational modification (PTM); protein acetyltransferase (PatZ or YfiQ)