Abstract：
: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 (CTDSaHPF). In this study, we solved the crystal structure of CTDSaHPF at 1.6 Å resolution and obtained a precise arrangement of the dimer interface. Residues Phe160, Val162, Thr171, Ile173, Tyr175, Ile185 andThr187 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 Phe160, Val162, Ile173, Tyr175 and Ile185 in the SaHPF homodimer interface abolished the ribosome dimerization in vitro.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
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 SZdoi
10.1016/j.jsb.2019.107408subject
Has Abstractpub_date
2020-01-01 00:00:00pages
107408issue
1eissn
1047-8477issn
1095-8657pii
S1047-8477(19)30229-1journal_volume
209pub_type
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