Skip Navigation



PEDS Advance Access published online on August 27, 2004
Protein Engineering Design and Selection, doi:10.1093/protein/gzh071
This Article
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
17/7/581    most recent
gzh071v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Zúñiga, R.
Right arrow Articles by Roth, M. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zúñiga, R.
Right arrow Articles by Roth, M. J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Received June 7, 2004
Revised August 18, 2004
Accepted August 20, 2004

Article

Expression of the C-terminus of HIV-1 reverse transcriptase P66 and P51 subunits as a single polypeptide with RNase H activity

Roberto Zúñiga 1, Sonali Sengupta 2, Christine Snyder , Oscar Leon 1, Monica J. Roth 2*

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

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


  Abstract

The C-terminus of the HIV-1 reverse transcriptase heterodimer has been 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 E. 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.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Protein Eng Des SelHome page
W. Wang, W. W. Prosise, J. Chen, S. S. Taremi, H. V. Le, V. Madison, X. Cui, A. Thomas, K.-C. Cheng, and C. A. Lesburg
Construction and characterization of a fully active PXR/SRC-1 tethered protein with increased stability
Protein Eng. Des. Sel., July 1, 2008; 21(7): 425 - 433.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
S. A. Gaidamakov, I. I. Gorshkova, P. Schuck, P. J. Steinbach, H. Yamada, R. J. Crouch, and S. M. Cerritelli
Eukaryotic RNases H1 act processively by interactions through the duplex RNA-binding domain
Nucleic Acids Res., April 14, 2005; 33(7): 2166 - 2175.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.