Home LiteratureArticle Details
PMID: 1741281 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Recognition nucleotides for human phenylalanyl-tRNA synthetase.

Nucleic acids research ·Vol. 20 ·No. 3 ·1992-02-11 ·Pages 475-8

Nazarenko IA, Peterson ET, Zakharova OD, Lavrik OI, Uhlenbeck OC

Abstract

The specificity of the interaction between tRNAPhe and phenylalanyl-tRNA synthetase isolated from human placenta was investigated. Using yeast tRNAPhe transcripts with different point mutations it was shown that all the five recognition points for the yeast phenylalanyl-tRNA synthetase (G20, G34, A35, A36 and A73) are also important for the reaction catalyzed by the human enzyme. A set of mutations in nucleotides involved in tertiary interactions of tRNAPhe revealed that mutations which maintained the proper folding of the molecule had almost no influence on the efficiency of aminoacylation. The most striking difference between the yeast and human phenylalanyl-tRNA synthetases involved a mutation in the lower two base pairs of the anticodon stem. This mutation did not affect aminoacylation with the yeast enzyme, but greatly reduced activity with human phenylalanyl-tRNA synthetase.

MeSH Terms
Anticodon/genetics Base Composition/genetics Base Sequence DNA Mutational Analysis Humans Kinetics Macromolecular Substances Molecular Sequence Data Nucleic Acid Conformation Phenylalanine-tRNA Ligase/metabolism RNA, Transfer, Phe/genetics,metabolism
Chemicals
Anticodon Macromolecular Substances RNA, Transfer, Phe Phenylalanine-tRNA Ligase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Nazarenko I A
Novosibirsk State University, Russia.
Peterson E T
Zakharova O D
Lavrik O I
Uhlenbeck O C
References (22)
22 references, click to expand
  1. Role of the tertiary nucleotides in the interaction of yeast phenylalanine tRNA with its cognate synthetase.
    Biochemistry. 1990 Mar 13;29(10):2523-32 PMID: 2334680
  2. Escherichia coli formylmethionine tRNA: mutations in GGGCCC sequence conserved in anticodon stem of initiator tRNAs affect initiation of protein synthesis and conformation of anticodon loop.
    Proc Natl Acad Sci U S A. 1987 Jan;84(2):334-8 PMID: 3540960
  3. Lead-catalyzed cleavage of yeast tRNAPhe mutants.
    Biochemistry. 1990 Mar 13;29(10):2515-23 PMID: 2334679
  4. Specific interaction of anticodon loop residues with yeast phenylalanyl-tRNA synthetase.
    Biochemistry. 1982 Aug 17;21(17):3921-6 PMID: 6751381
  5. Translational efficiency of transfer RNA's: uses of an extended anticodon.
    Science. 1982 Nov 12;218(4573):646-52 PMID: 6753149
  6. Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs.
    Annu Rev Biochem. 1979;48:601-48 PMID: 382994
  7. Studies on human tRNA. I. The rapid, large scale isolation and partial fractionation of placenta and liver tRNA.
    Nucleic Acids Res. 1975 Jan;2(1):21-42 PMID: 236551
  8. Sequence studies on tRNAPhe from placenta: comparison with known sequences of tRNAPhe from other normal mammalian tissues.
    Biochem Biophys Res Commun. 1975 Oct 27;66(4):1097-105 PMID: 1191278
  9. Recognition of tRNAs by aminoacyl-tRNA synthetases.
    Prog Nucleic Acid Res Mol Biol. 1991;41:23-87 PMID: 1882076
  10. [Phenylalanyl-tRNA-synthase from human placenta: isolation and characteristics].
    Biokhimiia. 1990 Jun;55(6):1025-31 PMID: 2207203
  11. Conversion of aminoacylation specificity from tRNA(Tyr) to tRNA(Ser) in vitro.
    Nucleic Acids Res. 1990 Dec 11;18(23):6815-9 PMID: 2263446
  12. Construction of two Escherichia coli amber suppressor genes: tRNAPheCUA and tRNACysCUA.
    Proc Natl Acad Sci U S A. 1986 Sep;83(17):6548-52 PMID: 3529087
  13. Evidence that a major determinant for the identity of a transfer RNA is conserved in evolution.
    Biochemistry. 1989 Aug 22;28(17):6800-4 PMID: 2684266
  14. Role of the extra G-C pair at the end of the acceptor stem of tRNA(His) in aminoacylation.
    Nucleic Acids Res. 1989 Oct 11;17(19):7855-63 PMID: 2678006
  15. Anticodon switching changes the identity of methionine and valine transfer RNAs.
    Science. 1988 Nov 4;242(4879):765-8 PMID: 3055296
  16. Nucleotides in yeast tRNAPhe required for the specific recognition by its cognate synthetase.
    Science. 1989 Mar 10;243(4896):1363-6 PMID: 2646717
  17. Aminoacylation of RNA minihelices with alanine.
    Nature. 1989 Feb 2;337(6206):478-81 PMID: 2915692
  18. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro.
    Proc Natl Acad Sci U S A. 1988 Feb;85(4):1033-7 PMID: 3277187
  19. Changing the identity of a transfer RNA.
    Nature. 1986 May 15-21;321(6067):213-9 PMID: 3086742
  20. Nucleotides that contribute to the identity of Escherichia coli tRNA(Phe).
    J Mol Biol. 1988 Aug 20;202(4):697-709 PMID: 2459397
  21. Changing the acceptor identity of a transfer RNA by altering nucleotides in a "variable pocket".
    Science. 1988 Sep 30;241(4874):1804-7 PMID: 2459773
  22. Relaxation of a transfer RNA specificity by removal of modified nucleotides.
    Nature. 1990 Apr 19;344(6268):787-9 PMID: 2330033
Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/20.3.475
Published
1992-02-11
Pages
475-8
Language
English
Region
England
NLM ID
0411011
PMCID
PMC310410
Subset
IM
Grants
NIGMS NIH HHS · GM37552 · United States
External Links
PubMed source DOI: 10.1093/nar/20.3.475 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2