Dimerization of long Hibernation Promoting Factor from Staphylococcus aureus: structural analysis and biochemical characterization.

Fiche publication

Date publication

octobre 2019

Journal

Journal of structural biology

Auteurs

Membres identifiés du Cancéropôle Est :
Dr YUSUPOV Marat

Tous les auteurs :
Usachev KS, Fatkhullin BF, Klochkova EA, Miftakhov AK, Golubev AA, Bikmullin AG, Nurullina LI, Garaeva NS, Islamov DR, Gabdulkhakov AG, Lekontseva NV, Tishchenko SV, Balobanov VA, Sh Khusainov I, Yusupov MM, Validov SZ

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/31669310

Résumé

Staphylococcus aureus hibernation promoting factor (SaHPF) is responsible for the formation of 100S ribosome dimers, which in turn help this pathogen to reduce energy spent under unfavorable conditions. Ribosome dimer formation strongly depends on the dimerization of the C-terminal domain of SaHPF (CTD). In this study, we solved the crystal structure of CTD at 1.6 Å resolution and obtained a precise arrangement of the dimer interface. Residues Phe, Val, Thr, Ile, Tyr, Ile andThr in the dimer interface of SaHPF protein were mutated and the effects were analyzed for the formation of 100S disomes of ribosomes isolated from S. aureus. It was shown that substitution of any of single residues Phe, Val, Ile, Tyr and Ile in the SaHPF homodimer interface abolished the ribosome dimerization in vitro.