FN Archimer Export Format
PT J
TI Pyrococcus horikoshii TET2 Peptidase Assembling Process and Associated Functional Regulation
BT 
AF APPOLAIRE, Alexandre
   ROSENBAUM, Eva
   DURA, M. Asuncion
   COLOMBO, Matteo
   MARTY, Vincent
   SAVOYE, Marjolaine Noirclerc
   GODFROY, Anne
   SCHOEHN, Guy
   GIRARD, Eric
   GABEL, Frank
   FRANZETTI, Bruno
AS 1:1,2,3;2:1,2,3;3:1,2,3;4:1,2,3;5:1,2,3;6:1,2,3;7:4;8:1,2,3;9:1,2,3;10:1,2,3;11:1,2,3;
FF 1:;2:;3:;4:;5:;6:;7:PDG-REM-EEP-LMEE;8:;9:;10:;11:;
C1 CNRS, Inst Biol Struct, UMR5075, F-38027 Grenoble, France.
   CEA Grenoble, F-38054 Grenoble, France.
   Univ Grenoble 1, F-38027 Grenoble, France.
   IFREMER, UMR6197, Lab Microbiol Environm Extremes, F-29280 Plouzane, France.
C2 CNRS, FRANCE
   CEA, FRANCE
   UNIV GRENOBLE, FRANCE
   IFREMER, FRANCE
SI BREST
SE PDG-REM-EEP-LMEE
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
IF 4.6
TC 11
UR https://archimer.ifremer.fr/doc/00177/28820/27491.pdf
LA English
DT Article
AB Tetrahedral (TET) aminopeptidases are large polypeptide destruction machines present in prokaryotes and eukaryotes. Here, the rules governing their assembly into hollow 12-subunit tetrahedrons are addressed by using TET2 from Pyrococcus horikoshii (PhTET2) as a model. Point mutations allowed the capture of a stable, catalytically active precursor. Small angle x- ray scattering revealed that it is a dimer whose architecture in solution is identical to that determined by x- ray crystallography within the fully assembled TET particle. Small angle x- ray scattering also showed that the reconstituted PhTET2 dodecameric particle displayed the same quaternary structure and thermal stability as the wild-type complex. The PhTET2 assembly intermediates were characterized by analytical ultracentrifugation, native gel electrophoresis, and electron microscopy. They revealed that PhTET2 assembling is a highly ordered process in which hexamers represent the main intermediate. Peptide degradation assays demonstrated that oligomerization triggers the activity of the TET enzyme toward large polypeptidic substrates. Fractionation experiments in Pyrococcus and Halobacterium cells revealed that, in vivo, the dimeric precursor co-exists together with assembled TET complexes. Taken together, our observations explain the biological significance of TET oligomerization and suggest the existence of a functional regulation of the dimer-dodecamer equilibrium in vivo.
PY 2013
PD AUG
SO Journal Of Biological Chemistry
SN 0021-9258
PU Amer Soc Biochemistry Molecular Biology Inc
VL 288
IS 31
UT 000330596300034
BP 22542
EP 22554
DI 10.1074/jbc.M113.450189
ID 28820
ER

EF