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Nucleic Acids Research, 1984, Vol. 12, No. 5 2259-2271
© 1984

ENZYMOLOGY

Interactions between avian myeloblastosis reverse transcriptase and tRNATrp. Mapping of complexed tRNA with chemicals and nucleases

Maurice Garret+, Pascale Romby*, Richard Giege* and Simon Litvak+

+Institut de Biochimie Cellulaire et Neurochimie du CNRS 1, rue Camille Saint Saëns, 33077 Bordeaux cedex *Institut de Biologie Moléculaire et Cellulaire du CNRS 15, rue Descartes, 67084 Strasbourg cedex, France

Received January 13, 1984. Accepted February 15, 1984.

The interactions between beef tNATrp with avian myeloblastosis reverse transcriptase have been studied by statistical chemical modifications of phosphate (ethylnitrosourea) and cytidine (dimethyl sulfate) residues, as well as by digestion of complexed tRNA by Cobra venom nuclease and Neurospora crassa endonuclease. Results with nucleases and chemicals show that reverse transcriptase interacts preferentially with the D arm, the anticodon stem and the T{psi} stem. All these regions are located in the outside of the L-shaped structure of tRNA. This domain of interaction is different to that reported previously in the complex of beef tRNA with the cognate aminoacyl-tRNA synthetase (M. Garret et al.; Eur. J. Biochem. In press). Avian reverse transcriptase destabilizes the region of tRNA where most of the tertiary interactions maintaining the structure of tRNA are located.


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[Abstract] [Full Text]


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