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  Structural and functional insights into human tRNA guanine transgylcosylase

Sievers, K., Welp, L., Urlaub, H., & Ficner, R. (2021). Structural and functional insights into human tRNA guanine transgylcosylase. RNA Biology, 18(Suppl. 1), 382-396. doi:10.1080/15476286.2021.1950980.

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Sievers, K., Author
Welp, L.1, Author           
Urlaub, H.1, Author           
Ficner, R., Author
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1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              

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Free keywords: Queuine; tRNA modification; RNA-binding protein; transglycosylase; heterodimer; eukaryotic; structural biology; X-ray crystallography
 Abstract: The eukaryotic tRNA guanine transglycosylase (TGT) is an RNA modifying enzyme incorporating queuine, a hypermodified guanine derivative, into the tRNAsAsp,Asn,His,Tyr. While both subunits of the functional heterodimer have been crystallized individually, much of our understanding of its dimer interface or recognition of a target RNA has been inferred from its more thoroughly studied bacterial homolog. However, since bacterial TGT, by incorporating queuine precursor preQ1, deviates not only in function, but as a homodimer, also in its subunit architecture, any inferences regarding the subunit association of the eukaryotic heterodimer or the significance of its unique catalytically inactive subunit are based on unstable footing. Here, we report the crystal structure of human TGT in its heterodimeric form and in complex with a 25-mer stem loop RNA, enabling detailed analysis of its dimer interface and interaction with a minimal substrate RNA. Based on a model of bound tRNA, we addressed a potential functional role of the catalytically inactive subunit QTRT2 by UV-crosslinking and mutagenesis experiments, identifying the two-stranded βEβF-sheet of the QTRT2 subunit as an additional RNA-binding motif.

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Language(s): eng - English
 Dates: 2021-07-312021
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1080/15476286.2021.1950980
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Title: RNA Biology
Source Genre: Journal
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Pages: - Volume / Issue: 18 (Suppl. 1) Sequence Number: - Start / End Page: 382 - 396 Identifier: ISSN: 1547-6286
ISSN: 1555-8584