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PMID: 2236077 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Enzymatic aminoacylation of an eight-base-pair microhelix with histidine.

Francklyn C, Schimmel P

Abstract

The major determinant for the identity of alanine tRNAs is a single base pair in the acceptor helix that is proximal to the site of amino acid attachment. A 7-base-pair microhelix that recreates the acceptor helix can be charged with alanine. No other examples of charging of small helices with specific amino acids have been reported, to our knowledge. We show here that a 13-base-pair and an 8-base-pair hairpin helix that reconstruct a domain and subdomain, respectively, of histidine tRNAs can be charged with histidine. We also show that transplantation of a base pair that is unique to histidine tRNAs is sufficient to consider histidine acceptance on a domain and subdomain of alanine tRNA. Both alanine and histidine aminoacyl-tRNA synthetases retain specificity for their cognate synthetic substrates. Alanine- and histidine-specific microhelices may resemble a system that arose early in the evolution of charging and coding.

MeSH Terms
Alanine-tRNA Ligase/metabolism Base Composition Base Sequence Histidine-tRNA Ligase/metabolism Kinetics Models, Molecular Molecular Sequence Data Nucleic Acid Conformation RNA, Transfer, Ala/genetics,metabolism RNA, Transfer, His/genetics,metabolism Substrate Specificity
Chemicals
RNA, Transfer, Ala RNA, Transfer, His Histidine-tRNA Ligase Alanine-tRNA Ligase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Francklyn C
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Schimmel P
References (30)
30 references, click to expand
  1. Evidence that the 3' end of a tRNA binds to a site in the adenylate synthesis domain of an aminoacyl-tRNA synthetase.
    Biochemistry. 1989 Mar 21;28(6):2577-86 PMID: 2543446
  2. 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
  3. Overproduction and dissection of proteins by the expression-cassette polymerase chain reaction.
    Proc Natl Acad Sci U S A. 1990 Mar;87(5):1937-41 PMID: 2408046
  4. A nucleotide that enhances the charging of RNA minihelix sequence variants with alanine.
    Biochemistry. 1990 Apr 17;29(15):3621-6 PMID: 1692733
  5. ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification.
    J Bacteriol. 1988 Mar;170(3):1245-53 PMID: 3277950
  6. Unusual CCA-stem structure of E. coli B tRNAH(His)(1).
    FEBS Lett. 1972 Jan 1;19(4):352-354 PMID: 11946249
  7. Changing the identity of a tRNA by introducing a G-U wobble pair near the 3' acceptor end.
    Science. 1988 May 6;240(4853):793-6 PMID: 2452483
  8. tRNA identity.
    Annu Rev Biochem. 1989;58:1029-49 PMID: 2673006
  9. 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
  10. Parameters for the molecular recognition of transfer RNAs.
    Biochemistry. 1989 Apr 4;28(7):2747-59 PMID: 2663057
  11. Structural homology in the amino-terminal domains of two aminoacyl-tRNA synthetases.
    J Mol Biol. 1983 Dec 25;171(4):571-6 PMID: 6363712
  12. Cloning and expression of the gene for bacteriophage T7 RNA polymerase.
    Proc Natl Acad Sci U S A. 1984 Apr;81(7):2035-9 PMID: 6371808
  13. The nucleotide sequence of the promoter region of hisS, the structural gene for histidyl-tRNA synthetase.
    Gene. 1982 May;18(2):107-14 PMID: 6290315
  14. Primary structure of histidine-tRNA synthetase and characterization of hisS transcripts.
    J Biol Chem. 1985 Aug 25;260(18):10063-8 PMID: 2991272
  15. Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution.
    Science. 1989 Dec 1;246(4934):1135-42 PMID: 2479982
  16. The anticodon contains a major element of the identity of arginine transfer RNAs.
    Science. 1989 Dec 22;246(4937):1595-7 PMID: 2688091
  17. Primary structure of a large aminoacyl-tRNA synthetase.
    Science. 1981 Sep 25;213(4515):1497-501 PMID: 7025207
  18. Synthesis of small RNAs using T7 RNA polymerase.
    Methods Enzymol. 1989;180:51-62 PMID: 2482430
  19. Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification.
    Nature. 1988 Nov 10;336(6195):179-81 PMID: 3054566
  20. Aminoacylation of RNA minihelices with alanine.
    Nature. 1989 Feb 2;337(6206):478-81 PMID: 2915692
  21. A simple structural feature is a major determinant of the identity of a transfer RNA.
    Nature. 1988 May 12;333(6169):140-5 PMID: 3285220
  22. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors.
    Gene. 1985;33(1):103-19 PMID: 2985470
  23. Relaxation of a transfer RNA specificity by removal of modified nucleotides.
    Nature. 1990 Apr 19;344(6268):787-9 PMID: 2330033
  24. Nucleotides in yeast tRNAPhe required for the specific recognition by its cognate synthetase.
    Science. 1989 Mar 10;243(4896):1363-6 PMID: 2646717
  25. Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold.
    J Mol Biol. 1982 Jul 15;158(4):699-709 PMID: 7120416
  26. Post-transcriptional nucleotide addition is responsible for the formation of the 5' terminus of histidine tRNA.
    Proc Natl Acad Sci U S A. 1982 Nov;79(21):6475-9 PMID: 6292903
  27. Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates.
    Nucleic Acids Res. 1987 Nov 11;15(21):8783-98 PMID: 3684574
  28. Understanding structural relationships in proteins of unsolved three-dimensional structure.
    Proteins. 1990;7(2):99-111 PMID: 2183216
  29. Anticodon switching changes the identity of methionine and valine transfer RNAs.
    Science. 1988 Nov 4;242(4879):765-8 PMID: 3055296
  30. Purification and characterization of histidyl transfer ribonucleic acid synthetase of Escherichia coli.
    Biochemistry. 1974 Feb 26;13(5):999-1006 PMID: 4591623
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1990-11-00
Pages
8655-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC55016
Subset
IM
Grants
NIGMS NIH HHS · GM 15539 · United States
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