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Victoriia Murina
Researcher at Umeå University
Publications - 22
Citations - 426
Victoriia Murina is an academic researcher from Umeå University. The author has contributed to research in topics: Translation (biology) & Transfer RNA. The author has an hindex of 10, co-authored 21 publications receiving 291 citations. Previous affiliations of Victoriia Murina include K L University & Russian Academy of Sciences.
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Journal ArticleDOI
ABCF ATPases Involved in Protein Synthesis, Ribosome Assembly and Antibiotic Resistance: Structural and Functional Diversification across the Tree of Life
Victoriia Murina,Marje Kasari,Hiraku Takada,Mariliis Hinnu,Chayan Kumar Saha,James W. Grimshaw,Takahiro Seki,Michael Reith,Marta Putrinš,Tanel Tenson,Henrik Strahl,Vasili Hauryliuk,Vasili Hauryliuk,Gemma C. Atkinson +13 more
TL;DR: The data suggest that there are a number of previously unidentified ARE ABCFs in antibiotic producers and important human pathogens, and 45 distinct subfamilies of ABCFs that are widespread across bacterial and eukaryotic phyla are found.
Journal ArticleDOI
Structural basis for antibiotic resistance mediated by the Bacillus subtilis ABCF ATPase VmlR.
Caillan Crowe-McAuliffe,Michael Graf,Paul Huter,Hiraku Takada,Maha Abdelshahid,Jiří Nováček,Victoriia Murina,Gemma C. Atkinson,Vasili Hauryliuk,Vasili Hauryliuk,Daniel N. Wilson +10 more
TL;DR: The study indicates that VmlR allosterically dissociates the drug from its ribosomal binding site and exhibits specificity to dislodge VgM, Lnc, and the pleuromutilin tiamulin (Tia), but not chloramphenicol (Cam), linezolid (Lnz), nor the macrolide erythromycin (Ery).
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Antibiotic resistance ABCF proteins reset the peptidyl transferase centre of the ribosome to counter translational arrest.
TL;DR: It is demonstrated that VgaALC is an NTPase that operates as a molecular machine strictly requiring NTP hydrolysis (not just NTP binding) for antibiotic protection, and when bound to the ribosome in the NTP-bound form, hydrolytically inactive EQ2ABCF ARE mutants inhibit peptidyl transferase activity, suggesting a direct interaction between the ABCF ARE and the PTC.
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The C-Terminal RRM/ACT Domain Is Crucial for Fine-Tuning the Activation of 'Long' RelA-SpoT Homolog Enzymes by Ribosomal Complexes.
Hiraku Takada,Mohammad Roghanian,Victoriia Murina,Ievgen Dzhygyr,Rikinori Murayama,Genki Akanuma,Gemma C. Atkinson,Abel Garcia-Pino,Vasili Hauryliuk,Vasili Hauryliuk +9 more
TL;DR: This work characterized Escherichia coli RelA and Bacillus subtilis Rel RSHs lacking RRM and demonstrated that the cytotoxicity caused by the removal of RRM is counteracted by secondary mutations that disrupt the interaction of the RSH with the starved ribosomal complex.
Journal ArticleDOI
Structural basis of ABCF-mediated resistance to pleuromutilin, lincosamide, and streptogramin A antibiotics in Gram-positive pathogens
Caillan Crowe-McAuliffe,Victoriia Murina,Kathryn Jane Turnbull,Marje Kasari,Merianne Mohamad,Christine Polte,Hiraku Takada,Karolis Vaitkevicius,Jörgen Johansson,Zoya Ignatova,Gemma C. Atkinson,Alex J. O'Neill,Vasili Hauryliuk,Daniel N. Wilson +13 more
TL;DR: In this article, the antibiotic resistance (ARE) ATP-binding cassette (ATP-CASS) was used as a target protection protein against resistance to the host organism by directly binding to the antibiotic target.