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».
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Biochimie, Elsevier, 2016, 122, pp.188-196. 〈10.1016/j.biochi.2015.11.001〉
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Soumis le : jeudi 7 avril 2016 - 08:37:19
Dernière modification le : lundi 19 février 2018 - 14:34:03

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Alexandre Appolaire, Matteo Colombo, Hind Basbous, Frank Gabel, Eric Girard, et al.. TET peptidases: A family of tetrahedral complexes conserved in prokaryotes. Biochimie, Elsevier, 2016, 122, pp.188-196. 〈10.1016/j.biochi.2015.11.001〉. 〈hal-01299014〉

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