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Publication Abstract from PubMed

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(SaHPF)). In this study, we solved the crystal structure of CTD(SaHPF) at 1.6A resolution and obtained a precise arrangement of the dimer interface. Residues Phe(160), Val(162), Thr(171), Ile(173), Tyr(175), Ile(185) andThr(187) 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(160), Val(162), Ile(173), Tyr(175) and Ile(185) in the SaHPF homodimer interface abolished the ribosome dimerization in vitro.

Dimerization of long hibernation promoting factor from Staphylococcus aureus: Structural analysis and biochemical characterization.,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, Khusainov IS, Yusupov MM, Validov SZ J Struct Biol. 2019 Oct 25:107408. doi: 10.1016/j.jsb.2019.107408. PMID:31669310^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.