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

Title data

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. Vol. 269 (1994) Issue 2 . - pp. 1388-1393.
ISSN 1083-351X

Official URL: Volltext

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers > Lehrstuhl Biopolymere - Apl. Prof. Dr. Birgitta Wöhrl
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 20 May 2019 11:38
Last Modified: 20 May 2019 11:38
URI: https://eref.uni-bayreuth.de/id/eprint/49003