JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on August 31, 2001
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
276/36/34213    most recent
M104632200v1
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Katz, R. A.
Right arrow Articles by Skalka, A. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Katz, R. A.
Right arrow Articles by Skalka, A. M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print July 5, 2001
J. Biol. Chem, 10.1074/jbc.M104632200
Submitted on May 21, 2001
Revised on July 5, 2001
Accepted on July 3, 2001

Role of DNA-end distortion in catalysis by avian sarcoma virus integrase

Richard A. Katz, Paul DiCandeloro, George Kukolj, and Anna Marie Skalka

Fox Chase Cancer Center, Philadelphia, PA 19111

Corresponding Author: r_katz{at}fccc.edu

Retroviral integrase (IN) recognizes linear viral DNA ends and introduces nicks adjacent to a highly conserved CA dinucleotide usually located two base pairs from the 3´-ends of viral DNA (the "processing" reaction). In a second step, the same IN active site catalyzes the insertion these ends into host DNA (the "joining" reaction). Both DNA sequence and DNA structure contribute to specific recognition of viral DNA ends by IN. Here we use potassium permanganate modification to show that the avian sarcoma virus (ASV) IN catalytic domain is able to distort viral DNA ends in vitro. This distortion activity is consistent with both unpairing and unstacking of the three terminal base pairs, including the processing site adjacent to the conserved CA. Furthermore, the introduction of mismatch mutations that destabilize the viral DNA ends were found to stimulate the IN processing reaction as well as IN-mediated distortion. End-distortion activity was also observed with mutant or heterologous DNA substrates. However, further analyses showed that using Mn2+ as a cofactor, processing site specificity of these substrates was also maintained. Our results support a model whereby unpairing and unstacking of the terminal base pairs is a required step in the processing reaction. Furthermore, these results are consistent with our previous observations indicating that unpairing of target DNA promotes the joining reaction.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
S. P. Montano, M. L. Cote, M. J. Roth, and M. M. Georgiadis
Crystal structures of oligonucleotides including the integrase processing site of the Moloney murine leukemia virus
Nucleic Acids Res., November 14, 2006; 34(19): 5353 - 5360.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Agapkina, M. Smolov, S. Barbe, E. Zubin, T. Zatsepin, E. Deprez, M. Le Bret, J.-F. Mouscadet, and M. Gottikh
Probing of HIV-1 Integrase/DNA Interactions Using Novel Analogs of Viral DNA
J. Biol. Chem., April 28, 2006; 281(17): 11530 - 11540.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
A. Narezkina, K. D. Taganov, S. Litwin, R. Stoyanova, J. Hayashi, C. Seeger, A. M. Skalka, and R. A. Katz
Genome-Wide Analyses of Avian Sarcoma Virus Integration Sites
J. Virol., November 1, 2004; 78(21): 11656 - 11663.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
K. Gao, S. Wong, and F. Bushman
Metal Binding by the D,DX35E Motif of Human Immunodeficiency Virus Type 1 Integrase: Selective Rescue of Cys Substitutions by Mn2+ In Vitro
J. Virol., July 1, 2004; 78(13): 6715 - 6722.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
R. Daniel, G. Kao, K. Taganov, J. G. Greger, O. Favorova, G. Merkel, T. J. Yen, R. A. Katz, and A. M. Skalka
Evidence that the retroviral DNA integration process triggers an ATR-dependent DNA damage response
PNAS, April 15, 2003; 100(8): 4778 - 4783.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Kvaratskhelia, S. R. Budihas, and S. F. J. Le Grice
Pre-existing Distortions in Nucleic Acid Structure Aid Polypurine Tract Selection by HIV-1 Reverse Transcriptase
J. Biol. Chem., May 3, 2002; 277(19): 16689 - 16696.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. K. Bao, A. M. Skalka, and I. Wong
Presteady-state Analysis of Avian Sarcoma Virus Integrase. I. A SPLICING ACTIVITY AND STRUCTURE-FUNCTION IMPLICATIONS FOR COGNATE SITE RECOGNITION
J. Biol. Chem., March 29, 2002; 277(14): 12089 - 12098.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. K. Bao, A. M. Skalka, and I. Wong
Presteady-state Analysis of Avian Sarcoma Virus Integrase. II. REVERSE-POLARITY SUBSTRATES IDENTIFY PREFERENTIAL PROCESSING OF THE U3-U5 PAIR
J. Biol. Chem., March 29, 2002; 277(14): 12099 - 12108.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.