Dimerization of long hibernation promoting factor from Staphylococcus aureus: Structural analysis and biochemical characterization

被引：6
作者：
Usachev, Konstantin S. [1 ]
Fatkhullin, Bulat F. [1 ,2 ]
Klochkova, Evelina A. [1 ]
Miftakhov, Aynur K. [1 ]
Golubev, Alexander A. [1 ]
Bikmullin, Aidar G. [1 ]
Nurullina, Liliya I. [1 ]
Garaeva, Natalia S. [1 ]
Islamov, Daut R. [1 ]
Gabdulkhakov, Azat G. [2 ]
Lekontseva, Natalia V. [2 ]
Tishchenko, Svetlana V. [2 ]
Balobanov, Vitaly A. [2 ]
Khusainov, Iskander Sh. [1 ,3 ,4 ]
Yusupov, Marat M. [1 ,3 ]
Validov, Shamil Z. [1 ]
机构：
[1] Kazan Fed Univ, Inst Fundamental Med cold Biol, Struct Biol Lab, 18 Kremlyovskaya, Kazan 420008, Russia
[2] Russian Acad Sci, Inst Prot Res, Inst Skaya 4, Pushchino 142290, Moscow Region, Russia
[3] Univ Strasbourg, Dept Biol & Genom Struct, Inst Genet & Biol Mol & Cellulaire, CNRS,UMR7104,INSERM,U964, 1 Rue Laurent Fries, F-67400 Illkirch Graffenstaden, France
[4] EMBL Heidelberg, Meyerhofstr 1, D-69117 Heidelberg, Germany
来源：
JOURNAL OF STRUCTURAL BIOLOGY | 2020年 / 209卷 / 01期
基金：
俄罗斯科学基金会;
关键词：
Ribosome; Staphylococcus aureus; Long HPF; Hibernation; X-ray; 100S RIBOSOME; PSEUDOMONAS-AERUGINOSA; STATIONARY-PHASE; FACTOR HOMOLOG; YFIA; SURVIVAL; YHBH;
D O I：
10.1016/j.jsb.2019.107408
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 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.
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页数：7
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