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PMID: 8335008 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

The EMBO journal ·Vol. 12 ·No. 7 ·1993-07-00 ·Pages 2949-57

Pütz J, Puglisi JD, Florentz C, Giegé R

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.

MeSH Terms
Acylation Aspartate-tRNA Ligase/metabolism Aspartic Acid/chemistry,genetics Base Sequence Catalysis Kinetics Molecular Sequence Data Mutation Nucleic Acid Conformation Nucleotides/metabolism RNA, Transfer, Asp/chemistry,genetics,metabolism Saccharomyces cerevisiae/enzymology
Chemicals
Nucleotides RNA, Transfer, Asp Aspartic Acid Aspartate-tRNA Ligase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Pütz J
Unité Structure des Macromolécules Biologiques et Mécanismes de Reconnaissance, Institut de Biologie Moléculaire et Cellulaire du Centre National de la Recherche Scientifique, Strasbourg, France.
Puglisi J D
Florentz C
Giegé R
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1993-07-00
Pages
2949-57
Language
English
Region
England
NLM ID
8208664
PMCID
PMC413550
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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