Author

V. Murina

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 4 Microbiology· 4

Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 6 Approach:experimental assay· 6 Assay:cryo-EM· 3 Research Focus:host-pathogen & immune response· 3 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Approach:microscopy & imaging analysis· 2

Frequent Co-Authors

V. Hauryliuk· 7 shared G. C. Atkinson· 6 shared H. Takada· 6 shared D. N. Wilson· 5 shared C. Crowe-McAuliffe· 4 shared C. Polte· 2 shared K. J. Turnbull· 2 shared M. Kasari· 2 shared

Activity by Year

2018-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 40 mutual co-author links

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7 shared papersMicrobiology

V. Hauryliuk

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Genome-encoded ABCF factors implicated in intrinsic antibiotic resistance in Gram-positive bacteria: VmlR2, Ard1 and CplR

N. Obana, H. Takada, C. Crowe-McAuliffe, M. Iwamoto, A. A. Egorov, K. J. Y. Wu, V. Murina, H. Paternoga, B. I. C. Tresco, N. Nomura, A. G. Myers, G. C. Atkinson, D. N. Wilson, V. Hauryliuk

The paper characterizes genome-encoded ABCF proteins in Gram-positive bacteria, showing their roles in intrinsic antibiotic resistance and revealing structural and regulatory mechanisms.

bioRxiv · Dec 5, 2022 · PreprintMicrobiology

Structural basis for PoxtA-mediated resistance to Phenicol and Oxazolidinone antibiotics

C. Crowe-McAuliffe, V. Murina, M. Kasari, H. Takada, K. J. Turnbull, Y. S. Polikanov, A. Sundsfjord, K. Hegstad, G. C. Atkinson, D. N. Wilson, V. Hauryliuk

This paper presents cryo-EM structures of PoxtA bound to the ribosome, revealing its mechanism of antibiotic resistance by perturbing tRNA and altering nascent chain conformation.

bioRxiv · Jun 18, 2021Microbiology

Structural basis of resistance to lincosamide, streptogramin A, and pleuromutilin antibiotics by ABCF ATPases in Gram-positive pathogens

C. Crowe-McAuliffe, V. Murina, K. J. Turnbull, M. Kasari, M. Mohamad, C. Polte, H. Takada, K. Vaitkevicius, J. Johansson, Z. Ignatova, G. C. Atkinson, A. C. O'Neill, V. Hauryliuk, D. N. Wilson

The paper determines the structures of ARE ABCF-ribosome complexes from three Gram-positive bacteria and proposes a model for antibiotic resistance mechanisms.

bioRxiv · Nov 24, 2020Microbiology

Hfq-assisted RsmA regulation is central to Pseudomonas aeruginosa biofilm polysaccharide PEL expression

Y. Irie, V. Murina, V. Hauryliuk, V. Shingler

The paper identifies Hfq-assisted RsmA regulation as critical for controlling PEL polysaccharide expression in Pseudomonas aeruginosa biofilms.

Frontiers in Microbiology · Nov 17, 2020Peer-reviewedMicrobiology

Structural basis for bacterial ribosome quality control

C. Crowe-McAuliffe, H. Takada, V. Murina, C. Polte, S. Kasvandik, T. Tenson, Z. Ignatova, G. C. Atkinson, D. N. Wilson, V. N. Hauryliuk

This study identifies RqcH and YabO as factors mediating C-terminal tailing in Bacillus subtilis through cryo-EM structures showing their role in tRNA movement without mRNA or small subunit.

bioRxiv · Sep 3, 2020Biochemistry

The C-terminal RRM/ACT domain is crucial for fine-tuning the activation of 'long' RelA-SpoT Homolog enzymes by ribosomal complexes

H. Takada, M. Roghanian, V. Murina, I. Dzhygyr, R. Murayama, G. Akanuma, G. C. Atkinson, A. Garcia-Pino, V. Hauryliuk

This study shows that the RRM domain in long RSH enzymes is essential for proper ribosome-mediated activation, preventing excessive (p)ppGpp production and cytotoxicity.

bioRxiv · Jan 23, 2020Biochemistry

A role for the Saccharomyces cerevisiae ABCF protein New1 during translation termination

V. Kasari, A. A. Pochopien, T. Margus, V. Murina, Y. Zhou, T. Nissan, M. Graf, J. Novacek, G. C. Atkinson, M. J. O. Johansson, D. N. Wilson, V. Hauryliuk

This study identifies New1 as a translation termination factor in yeast by showing it binds the ribosome like eEF3 and affects ribosome queuing at stop codons.

bioRxiv · May 14, 2019 · PreprintBiochemistry

Elimination of ribosome inactivating factors improves the efficiency of Bacillus subtilis and Saccharomyces cerevisiae cell-free translational systems

T. Brodiazhenko, M. Johansson, H. Takada, T. Nissan, V. Hauryliuk, V. Murina

This study shows that disrupting genes encoding ribosome inactivating factors improves the activity of cell-free translational systems in Bacillus subtilis and Saccharomyces cerevisiae.

bioRxiv · Sep 22, 2018Biochemistry