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Nucleic Acids Research, 1980, Vol. 8, No. 17 4009-4020
© 1980

ENZYMOLOGY

Study of the interactions between avian myeloblastosis virus reverse transcriptase and primer tRNA. Affinity labeling and inactivation of the enzyme by periodate-treated tRNATrp

Alejandro Araya, Edith Hevia and Simon Litvak{dagger}

Institut de Biochimie Cellulaire et Neurochimie, C.N.R.S. 1 Rue Camille Saint Saens, 33000 Bordeaux, France

{dagger}To whom all correspondence should be addressed

Received May 21, 1980. Reverse transcriptase from avian myeloblastosis virus can react with periodate-treated primer tRNATrP(beef) to form a Schiff's base between an {varepsilon}-NH2 lysine group whithin the active center of the enzyme and the dialdehyde derivative of the 3' terminal ribose of tRNA. In the presence of cyanoborohydride the reversible imminium moiety of the Schiff's base is reduced to a more stable adduct. Non-primer tRNAs were not able to reduce the extent of primer fixation to the enzyme.

Complete inactivation of the enzyme was attained when the ratio enzyme:tRNA in the complex was 1:1. When the 1:1 adduct was analyzed by polyacrylamide gel electrophoresis , radioactivity from the terminal adenosine of tRNA was found exclusively associated with the {alpha} subunit. At longer times of labeling the ß subunit was also found linked to the oxidized primer tRNA.


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