title: TET peptidases: A family of tetrahedral complexes conserved in prokaryotes.
abstract: The TET peptidases are large polypeptide destruction machines present among prokaryotes. They form 12-subunits hollow tetrahedral particles, and belong to the family of M42 metallo-peptidases. Structural characterization of various archaeal and bacterial complexes has revealed a unique mechanism of internal compartmentalization and peptide trafficking that distinguishes them from the other oligomeric peptidases. Different versions of the TET complex often co-exist in the cytosol of microorganisms. In depth enzymatic studies have revealed that they are non-processive cobalt-activated aminopeptidases and display contrasting substrate specificities based on the properties of the catalytic chambers. Recent studies have shed light on the assembly mechanism of homo and hetero-dodecameric TET complexes and shown that the activity of TET aminopeptidase towards polypeptides is coupled with its assembly process. These findings suggested a functional regulation based on oligomerization control in vivo. This review describes a current knowledge on M42 TET peptidases biochemistry and discuss their possible physiological roles. This article is a part of the Special Issue entitled: «A potpourri of proteases and inhibitors: from molecular toolboxes to signalling scissors».
authors.affiliation: CNRS, IBS, F-38027 Grenoble, France; CEA, DSV, IBS, F-38027 Grenoble, France; Univ. Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38027 Grenoble, France.
authors.forename: Alexandre
authors.initials: A
authors.lastname: Appolaire
authors.affiliation: CNRS, IBS, F-38027 Grenoble, France; CEA, DSV, IBS, F-38027 Grenoble, France; Univ. Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38027 Grenoble, France.
authors.forename: Matteo
authors.initials: M
authors.lastname: Colombo
authors.affiliation: CNRS, IBS, F-38027 Grenoble, France; CEA, DSV, IBS, F-38027 Grenoble, France; Univ. Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38027 Grenoble, France.
authors.forename: Hind
authors.initials: H
authors.lastname: Basbous
authors.affiliation: CNRS, IBS, F-38027 Grenoble, France; CEA, DSV, IBS, F-38027 Grenoble, France; Univ. Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38027 Grenoble, France.
authors.forename: Frank
authors.initials: F
authors.lastname: Gabel
authors.affiliation: CNRS, IBS, F-38027 Grenoble, France; CEA, DSV, IBS, F-38027 Grenoble, France; Univ. Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38027 Grenoble, France.
authors.forename: E
authors.initials: E
authors.lastname: Girard
authors.affiliation: CNRS, IBS, F-38027 Grenoble, France; CEA, DSV, IBS, F-38027 Grenoble, France; Univ. Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38027 Grenoble, France. Electronic address: franzetti@ibs.fr.
authors.forename: Bruno
authors.initials: B
authors.lastname: Franzetti
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011387:Prokaryotic Cells / Q000201:enzymology*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D008670:Metals; D000626:Aminopeptidases
keywords: Aminopeptidase; Intracellular proteolysis; Large molecular assemblies; M42; TET