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PEDS Advance Access originally published online on August 27, 2004
Protein Engineering Design and Selection 2004 17(7):581-587; doi:10.1093/protein/gzh071
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Protein Engineering, Design & Selection vol. 17 no. 7 © Oxford University Press 2004; all rights reserved

Expression of the C-terminus of HIV-1 reverse transcriptase p66 and p51 subunits as a single polypeptide with RNase H activity

Roberto Zúñiga1, Sonali Sengupta2, Christine Snyder2, Oscar Leon1 and Monica J. Roth2,3

1Programa de Virología, Instituto de Ciencias Biomédicas, Facultad de Medicina, Universidad de Chile, Independencia 1027, Santiago, Chile and 2Department of Biochemistry, University of Medicine and Dentistry of New Jersey–Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA

3 To whom correspondence should be addressed. E-mail: roth{at}waksman.rutgers.edu

The C-terminus of the HIV-1 reverse transcriptase heterodimer was reconstructed into a single polypeptide. The construct encodes the p51 thumb (T) and connection (C) subdomains joined through a linker region to the p66 connection (C) and RNase H (R) domain. The TCCR protein was purified from insoluble fractions of Escherichia coli lysates. The TCCR construct maintains Mn2+-dependent RNase H activity and specifically cleaves the substrate mimicking the tRNA removal required for second-strand transfer reactions.

Received June 7, 2004; revised August 18, 2004; accepted August 20, 2004.

Edited by Steven Russell


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