Functional Anticodon Architecture of Human tRNALys3 Includes Disruption of Intraloop Hydrogen Bonding by the Naturally Occurring Amino Acid Modification, t6A-Reference-Cited by-同舟云学术

Functional Anticodon Architecture of Human tRNALys3 Includes Disruption of Intraloop Hydrogen Bonding by the Naturally Occurring Amino Acid Modification, t6A

Published:2000-10-10 Issue:44 Volume:39 Page:13396-13404
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Stuart John W.¹,Gdaniec Zofia¹,Guenther Richard¹,Marszalek Michal¹,Sochacka Elzbieta¹,Malkiewicz Andrzej¹,Agris Paul F.¹

Affiliation:

1. Department of Biochemistry, North Carolina State University, Raleigh, North Carolina 27695-7622, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan 61-704, Poland, and Institute of Organic Chemistry, Technical University, Lodz 90-924, Poland

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0013039

Reference55 articles.

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2. Missense misreading of asparagine codons as a function of codon identity and context.

3. Reduced misreading of asparagine codons by Escherichia coli tRNA Lys with hypomodified derivatives of 5-methylaminomethyl-2-thiouridine in the wobble position 1 1Edited by D. E. Draper

4. The growth defect in Escherichia coli deficient in peptidyl-tRNA hydrolase is due to starvation for Lys-tRNA(Lys).

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