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Biochimie. 2016 Mar;122:188-96. doi: 10.1016/j.biochi.2015.11.001. Epub 2015 Nov 4.

TET peptidases: A family of tetrahedral complexes conserved in prokaryotes.

Author information

1
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.
2
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.

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».

KEYWORDS:

Aminopeptidase; Intracellular proteolysis; Large molecular assemblies; M42; TET

PMID:
26546839
DOI:
10.1016/j.biochi.2015.11.001
[Indexed for MEDLINE]

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