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J Struct Biol. 2020 Jan 1;209(1):107408. doi: 10.1016/j.jsb.2019.107408. Epub 2019 Oct 25.

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

Author information

1
Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan 420008, Russian Federation.
2
Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan 420008, Russian Federation; Institute of Protein Research, Russian Academy of Sciences, Institutskaya 4, 142290 Puschino, Moscow Region, Russian Federation.
3
Institute of Protein Research, Russian Academy of Sciences, Institutskaya 4, 142290 Puschino, Moscow Region, Russian Federation.
4
Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan 420008, Russian Federation; Département de Biologie et de Génomique Structurales, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS UMR7104, INSERM U964, Université de Strasbourg, 1 rue Laurent Fries, F-67400 Illkirch, France.
5
Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan 420008, Russian Federation; Département de Biologie et de Génomique Structurales, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS UMR7104, INSERM U964, Université de Strasbourg, 1 rue Laurent Fries, F-67400 Illkirch, France. Electronic address: marat.yusupov@igbmc.fr.
6
Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan 420008, Russian Federation. Electronic address: szvalidov@kpfu.ru.

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.

KEYWORDS:

Hibernation; Long HPF; Ribosome; Staphylococcus aureus; X-ray

PMID:
31669310
DOI:
10.1016/j.jsb.2019.107408

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