Author

D. N. Wilson

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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Approach:experimental assay· 7 Organism:bacteria (other)· 4 Assay:cryo-EM· 4 Research Focus:protein folding & dynamics· 4 Research Focus:cell signaling & trafficking· 3 Research Focus:host-pathogen & immune response· 3 Research Focus:cell type annotation· 2 Approach:microscopy & imaging analysis· 2

Frequent Co-Authors

G. C. Atkinson· 6 shared H. Takada· 5 shared V. Hauryliuk· 5 shared V. Murina· 5 shared C. Crowe-McAuliffe· 4 shared B. Beckert· 3 shared T. Tenson· 3 shared A. A. Pochopien· 2 shared

Activity by Year

2019-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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6 shared papersMicrobiology

G. C. Atkinson

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Author profile →

8 papers

Recent·Most cited

A role for the S4-domain containing protein YlmH in ribosome-associated quality control in Bacillus subtilis

H. Takada, H. Paternoga, K. Fujiwara, J. A. Nakamoto, E. N. Park, L. Dimitrova-Paternoga, B. Beckert, M. Saarma, T. Tenson, A. Buskirk, G. C. Atkinson, S. Chiba, D. N. Wilson, V. Hauryliuk

This study identifies YlmH as a novel RQC factor in B. subtilis, showing it can replace RqcP in polyalanine tail addition and is conserved in bacteria lacking RqcP.

bioRxiv · Mar 3, 2024 · PreprintMicrobiology

Structural basis for translation inhibition 1 by the glycosylated antimicrobial peptide Drosocin from Drosophila melanogaster

T. O. Koller, M. Morici, M. Berger, H. Safdari, D. S. Lele, B. Beckert, K. J. Kaur, D. N. Wilson

This study reveals how O-glycosylation of drosocin affects its interaction with the ribosome, inhibiting translation by trapping RF1 in the exit tunnel.

bioRxiv · Dec 8, 2022 · PreprintBiochemistry

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

Structure of Gcn1 bound to stalled and colliding 80S ribosomes

A. A. Pochopien, B. Beckert, S. Kasvandik, O. Berninghausen, R. Beckmann, T. Tenson, D. N. Wilson

This study presents a cryo-EM structure of yeast Gcn1 bound to stalled and colliding 80S ribosomes, revealing its interaction with ribosomes and the role of Rbg2/Gir2 in repressing Gcn2.

bioRxiv · Oct 31, 2020Biochemistry

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

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