Purine bases at position 37 of tRNA stabilize codon-anticodon interaction in the ribosomal A site by stacking and Mg2+-dependent interactions. Konevega, A., Soboleva, N., Makhno, V., Semenkov, Y., Wintermeyer, W., Rodnina, M., & Katunin, V. RNA, 10(1):90-101, 2004. cited By 73![Purine bases at position 37 of tRNA stabilize codon-anticodon interaction in the ribosomal A site by stacking and Mg2+-dependent interactions [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The anticodon loop of tRNA contains a number of conserved or semiconserved nucleotides. In most tRNAs, a highly modified purine is found at position 37 immediately 3′ to the anticodon. Here, we examined the role of the base at position 37 for tRNAPhe binding to the A site of Escherichia coli ribosomes. Affinities and rate constants of A-site binding of native yeast peptidyl-tRNAPhe with hypermodified G (wybutine), or of unmodified peptidyl-tRNAPhe transcripts with G, A, C, or U, at position 37 were measured. The data indicate that purines stabilize binding due to stronger stacking and additional interactions with the ribosome mediated by Mg 2+ ions. Paromomycin, an antibiotic that binds to 16S rRNA in the decoding center, greatly stabilized tRNAs in the A site and abolished the Mg2+ -dependence of binding. Comparison of binding enthalpies and entropies suggests that hypermodification of the base at position 37 does not affect stacking in the codon-anticodon complex, but rather decreases the entropic penalty for A-site binding. Substitution of purines with pyrimidines at position 37 increases the rates of tRNA binding to and dissociation from the A site. The data suggest that initial binding of tRNA to the A site is followed by a rate-limiting rearrangement of the anticodon loop or the ribosome decoding center that is favored by purines at position 37 and involves stronger stacking, additional Mg2+ binding, and interactions with 16S rRNA.
@ARTICLE{Konevega200490,
author={Konevega, A.L. and Soboleva, N.G. and Makhno, V.I. and Semenkov, Y.P. and Wintermeyer, W. and Rodnina, M.V. and Katunin, V.I.},
title={Purine bases at position 37 of tRNA stabilize codon-anticodon interaction in the ribosomal A site by stacking and Mg2+-dependent interactions},
journal={RNA},
year={2004},
volume={10},
number={1},
pages={90-101},
doi={10.1261/rna.5142404},
note={cited By 73},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347623198&doi=10.1261%2frna.5142404&partnerID=40&md5=c0ac9c400bbb3e2d3a57147153225962},
affiliation={Petersburg Nuclear Physics Institute, Russian Academy of Sciences, 188300 Gatchina, Russian Federation; Institute of Molecular Biology, University of Witten/Herdecke, 58448 Witten, Germany; Institute of Physical Biochemistry, University of Witten/Herdecke, 58448 Witten, Germany},
abstract={The anticodon loop of tRNA contains a number of conserved or semiconserved nucleotides. In most tRNAs, a highly modified purine is found at position 37 immediately 3′ to the anticodon. Here, we examined the role of the base at position 37 for tRNAPhe binding to the A site of Escherichia coli ribosomes. Affinities and rate constants of A-site binding of native yeast peptidyl-tRNAPhe with hypermodified G (wybutine), or of unmodified peptidyl-tRNAPhe transcripts with G, A, C, or U, at position 37 were measured. The data indicate that purines stabilize binding due to stronger stacking and additional interactions with the ribosome mediated by Mg 2+ ions. Paromomycin, an antibiotic that binds to 16S rRNA in the decoding center, greatly stabilized tRNAs in the A site and abolished the Mg2+ -dependence of binding. Comparison of binding enthalpies and entropies suggests that hypermodification of the base at position 37 does not affect stacking in the codon-anticodon complex, but rather decreases the entropic penalty for A-site binding. Substitution of purines with pyrimidines at position 37 increases the rates of tRNA binding to and dissociation from the A site. The data suggest that initial binding of tRNA to the A site is followed by a rate-limiting rearrangement of the anticodon loop or the ribosome decoding center that is favored by purines at position 37 and involves stronger stacking, additional Mg2+ binding, and interactions with 16S rRNA.},
author_keywords={Ribosome decoding; Translation; TRNA conformational change; TRNA modifications; TRNA selection},
correspondence_address1={Katunin, V.I.; Petersburg Nuclear Physics Institute, Russian Academy of Sciences, 188300 Gatchina, Russian Federation; email: katunin@omrb.pnpi.spb.ru},
issn={13558382},
coden={RNARF},
pubmed_id={14681588},
language={English},
abbrev_source_title={RNA},
document_type={Article},
source={Scopus},
}
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In most tRNAs, a highly modified purine is found at position 37 immediately 3′ to the anticodon. Here, we examined the role of the base at position 37 for tRNAPhe binding to the A site of Escherichia coli ribosomes. Affinities and rate constants of A-site binding of native yeast peptidyl-tRNAPhe with hypermodified G (wybutine), or of unmodified peptidyl-tRNAPhe transcripts with G, A, C, or U, at position 37 were measured. The data indicate that purines stabilize binding due to stronger stacking and additional interactions with the ribosome mediated by Mg 2+ ions. Paromomycin, an antibiotic that binds to 16S rRNA in the decoding center, greatly stabilized tRNAs in the A site and abolished the Mg2+ -dependence of binding. Comparison of binding enthalpies and entropies suggests that hypermodification of the base at position 37 does not affect stacking in the codon-anticodon complex, but rather decreases the entropic penalty for A-site binding. Substitution of purines with pyrimidines at position 37 increases the rates of tRNA binding to and dissociation from the A site. 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