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

Publikováno v: 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⟩

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 formatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78cefd1383a536f1a4480a9a89686b36
https://hal.archives-ouvertes.fr/hal-03489916

Backbone and side chain NMR assignments for the ribosome binding factor A (RbfA) from Staphylococcus aureus

Autor: Dmitriy S, Blokhin, Aydar G, Bikmullin, Liliya I, Nurullina, Natalia S, Garaeva, Shamil Z, Validov, Vladimir V, Klochkov, Albert V, Aganov, Iskander Sh, Khusainov, Marat M, Yusupov, Konstantin S, Usachev

Publikováno v: Biomolecular NMR assignments. 13(1)

Ribosome binding factor A (RbfA) is a 14.9 kDa adaptive protein of cold shock, which is important for bacterial growth at low temperatures. RbfA can bind to the free 30S ribosomal subunit and interacts with the 5'-terminal helix (helix I) of 16S rRNA

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::65d4dcc864aea4a5ac253c56a1bae099
https://pubmed.ncbi.nlm.nih.gov/30225569