PMID:7698334

Citation	Mueller, SO and Slany, RK (1995) Structural analysis of the interaction of the tRNA modifying enzymes Tgt and QueA with a substrate tRNA. FEBS Lett. 361:259-64
Abstract	The enzymes tRNA guanine-transglycosylase (Tgt) and S-adenosylmethionine :tRNA ribosyltransferase-isomerase (QueA) participate in the biosynthesis of the hypermodified tRNA nucleoside queuosine (Q) in Escherichia coli. Here we show by HPLC analysis and gel retardation that both enzymes interact with an in vitro transcribed tRNA(ASP) from yeast, specifically modified with a Q precursor molecule. RNase I footprinting experiments showed strong protein tRNA contacts in the anticodon stem-loop and a minor interaction with the dihydrouridine loop. This suggests that all identity elements for the recognition of Q-specific tRNAs are clustered in the anticodon region and explains earlier results that both enzymes accept a RNA microhelix with the sequence of an anticodon stem-loop as substrate.
Links	PubMed
Keywords	Anticodon; Base Sequence; Binding Sites; Chromatography, High Pressure Liquid; Escherichia coli/enzymology; Escherichia coli/metabolism; Isomerases; Nucleic Acid Conformation; Nucleoside Q/biosynthesis; Pentosyltransferases/chemistry; Pentosyltransferases/metabolism; Protein Conformation; RNA, Transfer, Asp/biosynthesis; RNA, Transfer, Asp/chemistry; RNA, Transfer, Asp/metabolism; Saccharomyces cerevisiae/metabolism; Transcription, Genetic
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.