Products Cited in Publications Worldwide Structural and functional investigation of tRNA guanine transglycosylase

Structural and functional investigation of tRNA guanine transglycosylase

Katharina Sievers

DOI:

Abstract

The eukaryotic tRNA guanine transglycosylase (TGT) is an RNA modifying enzyme incorporating queuinea hypermodified guanine derivative, into the tRN AsAsp,Asn.His,Ty,. While both subunits of the functionaheterodimer have been crystalized individually, much of our understanding of its dimer interface orrecognition of a target RNA has been inferred from its more thoroughly studied bacterial homologHowever, since bacterial TGT, by incorporating queuine precursor preQ,, deviates not only in functionbut as a homodimer, also in its subunit architecture, any inferences regarding the subunit association ofthe eukaryotic heterodimer or the significance of its unique catalytically inactive subunit are based onunstable footing. Here, we report the crystal structure of human TGT in its heterodimeric form and incomplex with a 25-mer stem loop RNA, enabling detailed analysis of its dimer interface and interactionwith a minimal substrate RNA. Based on a model of bound tRNA, we addressed a potential functionalrole of the catalytically inactive subunit QTRT2 by UV-crosslinking and mutagenesis experimentsidentifying the two-stranded BEBF-sheet of the OTRT2 subunit as an additional RNA-binding motif.

Keywords

Queuine ; tRNA modifcation ; RN A-binding protein ; transglycosylase ; heterodimer ; eukaryotic ; structural biology ; X-raycrystallography

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9-Deazaguanine

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9-Deazaguanine

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