Clustering of OB-fold domains of the partner protease complexed with trimeric stomatin from Thermococcales. - I2BC Accéder directement au contenu
Article Dans Une Revue Biochimie Année : 2013

Clustering of OB-fold domains of the partner protease complexed with trimeric stomatin from Thermococcales.

Hideshi Yokoyama
  • Fonction : Auteur
Eriko Matsui
  • Fonction : Auteur
Kana Hiramoto
  • Fonction : Auteur
Ikuo Matsui
  • Fonction : Auteur

Résumé

The C-terminal soluble domain of stomatin operon partner protein (STOPP) of the hyperthermophilic archaeon Pyrococcus horikoshii has an oligonucleotide binding-fold (OB-fold). STOPP lacks the conserved surface residues necessary for binding to DNA/RNA. A tryptophan (W) residue is conserved instead at the molecular surface. Solvent-accessible W residues are often found at interfaces of protein-protein complexes, which suggested the possibility of self-assembling of STOPP. Protein-protein interactions among the C-terminal soluble domains of STOPP PH1510 (1510-C) were then analyzed by chemical linking and blue native polyacrylamide gel electrophoresis (BN-PAGE) methods. These results suggest that the soluble domains of STOPP could assemble into homo-oligomers. Since hexameric subcomplex I from archaeal proteasome consists of coiled-coil segments and OB-fold domains, molecular modeling of 1510-C was performed using hexameric subcomplex I as a template. Although 1510-C is a comparatively small polypeptide consisting of approximately 60 residues, numerous salt bridges and hydrophobic interactions were observed in the predicted hexamer of 1510-C, suggesting the stability of the homo-oligomeric structure. This oligomeric property of STOPP may be favorable for triplicate proteolysis of the trimer of prokaryotic stomatin.

Dates et versions

hal-00832131 , version 1 (10-06-2013)

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Citer

Hideshi Yokoyama, Eriko Matsui, Kana Hiramoto, Patrick Forterre, Ikuo Matsui. Clustering of OB-fold domains of the partner protease complexed with trimeric stomatin from Thermococcales.. Biochimie, 2013, 95 (7), pp.1494-501. ⟨10.1016/j.biochi.2013.04.002⟩. ⟨hal-00832131⟩
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