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Covalent complex of phenylalanyl-tRNA synthetase with 4-thiouridine-substituted tRNAPhegene transcript retains aminoacylation activity1 This manuscript was accepted for publication on 7 February 1998. Delay in publication is caused by mailing problems.1

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
427
Issue
1
Identifiers
DOI: 10.1016/s0014-5793(98)00398-6
Keywords
  • Protein-Nucleic Acid Recognition
  • Phenylalanyl-Trna Synthetase
  • Affinity Labeling
  • 4-Thiouridine
  • Thermus Thermophilus
Disciplines
  • Biology

Abstract

Abstract s 4U-containing transcripts of tRNA Phe gene have been prepared by complete substitution of 16 U residues or by random incorporation of s 4U residues followed by affinity electrophoresis isolation of s 4U-monosubstituted tRNA transcripts. Both analogs have been cross-linked to Thermus thermophilus phenylalanyl-tRNA synthetase (PheRS) and the specificity of the cross-linking has been demonstrated. Functional activity of the covalent complex of PheRS with the s 4U-monosubstituted transcript has been shown by aminoacylation of 60% of the enzyme-cross-linked tRNA. This is the first instance in which biological activity of aminoacyl-tRNA synthetase and cross-linked tRNA in a specific complex has been revealed.

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