Dimerization of long hibernation promoting factor from Staphylococcus aureus: Structural analysis and biochemical characterization
| Autor: | Konstantin S. Usachev, Bulat F. Fatkhullin, Evelina A. Klochkova, Aynur K. Miftakhov, Alexander A. Golubev, Aidar G. Bikmullin, Liliya I. Nurullina, Natalia S. Garaeva, Daut R. Islamov, Azat G. Gabdulkhakov, Natalia V. Lekontseva, Svetlana V. Tishchenko, Vitaly A. Balobanov, Iskander Sh. Khusainov, Marat M. Yusupov, Shamil Z. Validov |
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| Přispěvatelé: | Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), CCSD, Accord Elsevier, Kazan Federal University (KFU), Russian Academy of Sciences [Moscow] (RAS), Centre for Integrative Biology - CBI (Inserm U964 - CNRS UMR7104 - IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Ribosomal Proteins
0303 health sciences Staphylococcus aureus [SDV]Life Sciences [q-bio] 030302 biochemistry & molecular biology Cryoelectron Microscopy Staphylococcal Infections Long HPF Ribosome X-ray [SDV] Life Sciences [q-bio] 03 medical and health sciences Bacterial Proteins Structural Biology Hibernation Humans Dimerization Ribosomes 030304 developmental biology Protein Binding |
| Zdroj: | Journal of Structural Biology Journal of Structural Biology, Elsevier, 2020, 209, pp.107408-. ⟨10.1016/j.jsb.2019.107408⟩ Journal of Structural Biology, 2020, 209 (1), pp.107408-. ⟨10.1016/j.jsb.2019.107408⟩ |
| ISSN: | 1047-8477 1095-8657 |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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