Modulation of HIV-1 reverse transcriptase function in "selectively deleted" p66/p51 heterodimers

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Jacques, Pamela S. ; Wöhrl, Birgitta M. ; Howard, Kathryn J. ; Le Grice, Stuart F.J.:
Modulation of HIV-1 reverse transcriptase function in "selectively deleted" p66/p51 heterodimers.
In: The Journal of Biological Chemistry. Bd. 269 (1994) Heft 2 . - S. 1388-1393.
ISSN 1083-351X

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Abstract

A contribution of the 51-kDa subunit of human immunodeficiency virus type-1 reverse transcriptase to activities of the parental heterodimer (p66/p51) was assessed in "selectively deleted" heterodimers whose p51 component contained C-terminal truncations of 13, 19, or 25 residues. Analyses included (i) efficiency of reconstitution into heterodimer, (ii) retention of polymerase and ribonuclease H (RNase H) function, and (iii) interaction with the HIV replication primer, tRNA(Lys,3). Our data suggest that these features of heterodimer reverse transcriptase can be modulated by the extent of the C-terminal p51 deletion. Severely impaired tRNA binding in a selectively deleted heterodimer whose 51-kDa subunit lacks 13 residues, despite retention of enzymatic functions, strengthens arguments for p51 involvement in tRNA binding.