New photoactivatable structural and affinity probes of RNAs: specific features and applications for mapping of spermine binding sites in yeast tRNAAspand interaction of this tRNA with yeast aspartyl-tRNA synthetase
Open Access
- 11 January 1990
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 18 (1) , 89-95
- https://doi.org/10.1093/nar/18.1.89
Abstract
Aryldiazonium salts are shown to be useful as phototriggered structural probes for RNA mapping as well as for footprinting of RNA/protein interaction. In particular the yeast tRNAAsp/aspartyl-tRNA synthetase complex is shown to involve the variable loop face and the concave side of the L-shaped nucleic acid bound to a lipophilic area of the enzyme. When chemically linked to spermine, the photoactive group cleaves RNA at polyamine binding sites ; 3–4 spermines have been located in the tRNAAsp, stabilizing the central part of the molecule in regions where two ribose-phosphate strands are close to each other.Keywords
This publication has 33 references indexed in Scilit:
- A high resolution diffracting crystal form of the complex between yeast tRNAAsp and aspartyl-tRNA synthetaseJournal of Molecular Biology, 1988
- Comparison of the tertiary structure of yeast tRNAAsp and tRNAPhe in solutionJournal of Molecular Biology, 1987
- Spermine–nucleic acid interactions: A theoretical studyBiopolymers, 1986
- Nuclear magnetic resonance studies of polyamine binding to a defined DNA sequenceJournal of Molecular Biology, 1985
- Yeast tRNAAsp tertiary structure in solution and areas of interaction of the tRNA with aspartyl-tRNA synthetaseJournal of Molecular Biology, 1985
- Crystallographic refinement of yeast aspartic acid transfer RNAJournal of Molecular Biology, 1985
- Large scale purification and structural properties of yeast aspartyl-tRNA synthetaseBiochemical and Biophysical Research Communications, 1983
- Formation of a catalytically active complex between tRNAAsp and aspartyl-tRNA synthetase from yeast in high concentrations of ammonium sulphateBiochimie, 1982
- PHOTOLYTIC INHIBITION AND LABELING OF PROTEINS WITH ARYL DIAZONIUM COMPOUNDSInternational Journal of Peptide and Protein Research, 1978
- Binding of transfer rna to polyamines in preference to Mg2+Biochemical and Biophysical Research Communications, 1975