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Jul, 1993;12 (7): 2949-57.

Additive, cooperative and anti-cooperative effects between identity nucleotides of a tRNA.

J Pütz, J D Puglisi, C Florentz, R Giegé
Author Information
  1. J Pütz: Unité Structure des Macromolécules Biologiques et Mécanismes de Reconnaissance, Institut de Biologie Moléculaire et Cellulaire du Centre National de la Recherche Scientifique, Strasbourg, France.
PMID: 8335008 DOI: 10.1002/j.1460-2075.1993.tb05957.x

Abstract

We have investigated the functional relationship between nucleotides in yeast tRNAAsp that are important for aspartylation by yeast aspartyl-tRNA synthetase. Transcripts of tRNAAsp with two or more mutations at identity positions G73, G34, U35, C36 and base pair G10-U25 have been prepared and the steady-state kinetics of their aspartylation were measured. Multiple mutations affect the catalytic activities of the synthetase mainly at the level of the catalytic constant, kcat. Kinetic data were expressed as free energy variation at transition state of these multiple mutants and comparison of experimental values with those calculated from results on single mutants defined three types of relationships between the identity nucleotides of this tRNA. Nucleotides located far apart in the three-dimensional structure of the tRNA act cooperatively whereas nucleotides of the anticodon triplet act either additively or anti-cooperatively. These results are related to the specific interactions of functional groups on identity nucleotides with amino acids in the protein as revealed by the crystal structure of the tRNAAsp/aspartyl-tRNA synthetase complex. These relationships between identity nucleotides may play an important role in the biological function of tRNAs.

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MeSH Term

Acylation
Aspartate-tRNA Ligase
Aspartic Acid
Base Sequence
Catalysis
Kinetics
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
Nucleotides
RNA, Transfer, Asp
Saccharomyces cerevisiae

Chemicals

Nucleotides
RNA, Transfer, Asp
Aspartic Acid
Aspartate-tRNA Ligase
Journal Article Research Support, Non-U.S. Gov't

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