JBC Origene Your Gene Company

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


     

A more recent version of this article appeared on April 15, 2005
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
280/15/15212    most recent
M500108200v1
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 Perrino, F. W.
Right arrow Articles by Hollis, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Perrino, F. W.
Right arrow Articles by Hollis, T.
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 January 19, 2005
J. Biol. Chem, 10.1074/jbc.M500108200
Submitted on January 4, 2005
Revised on January 19, 2005
Accepted on January 19, 2005

The human TREX2 3'-5' exonuclease structure suggests a mechanism for efficient non-processive DNA catalysis

Fred W. Perrino, Scott Harvey, Sara McMillin, and Thomas Hollis

Biochemistry Dept., Wake Forest University School of Medicine, Winston-Salem, NC 27157

Corresponding Author: thollis{at}wfubmc.edu

The 3'-5' exonucleases process DNA ends in many DNA repair pathways of human cells. Determination of the human TREX2 structure is the first of a dimeric 3' deoxyribonuclease, and indicates how this highly efficient non-processive enzyme removes nucleotides at DNA 3' termini. Symmetry in the TREX2 dimer positions the active sites at opposite outer edges providing open access for the DNA. Adjacent to each active site is a flexible region containing three arginines appropriately positioned to bind DNA and to control its entry into the active site. Mutation of these three arginines to alanines reduces the DNA binding capacity by ~100-fold with no effect on catalysis. The human TREX2 catalytic residues overlay with the bacterial DnaQ family of 3' exonucleases confirming the structural conservation of the catalytic sites despite limited sequence identity and mutations of these residues decrease the still measurable activity by ~105-fold confirming their catalytic role.


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
 J. Biol. Chem.Home page
F. W. Perrino, U. de Silva, S. Harvey, E. E. Pryor Jr., D. W. Cole, and T. Hollis
Cooperative DNA Binding and Communication across the Dimer Interface in the TREX2 3' -> 5'-Exonuclease
J. Biol. Chem., August 1, 2008; 283(31): 21441 - 21452.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Brucet, J. Querol-Audi, M. Serra, X. Ramirez-Espain, K. Bertlik, L. Ruiz, J. Lloberas, M. J. Macias, I. Fita, and A. Celada
Structure of the Dimeric Exonuclease TREX1 in Complex with DNA Displays a Proline-rich Binding Site for WW Domains
J. Biol. Chem., May 11, 2007; 282(19): 14547 - 14557.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M.-J. Chen, S.-M. Ma, L. C. Dumitrache, and P. Hasty
Biochemical and cellular characteristics of the 3' -> 5' exonuclease TREX2
Nucleic Acids Res., April 10, 2007; (2007) gkm151v1.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
U. de Silva, S. Choudhury, S. L. Bailey, S. Harvey, F. W. Perrino, and T. Hollis
The Crystal Structure of TREX1 Explains the 3' Nucleotide Specificity and Reveals a Polyproline II Helix for Protein Partnering
J. Biol. Chem., April 6, 2007; 282(14): 10537 - 10543.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. W. Kirby, S. Harvey, E. F. DeRose, S. Chalov, A. K. Chikova, F. W. Perrino, R. M. Schaaper, R. E. London, and L. C. Pedersen
Structure of the Escherichia coli DNA Polymerase III {epsilon}-HOT Proofreading Complex
J. Biol. Chem., December 15, 2006; 281(50): 38466 - 38471.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
E. Minskaia, T. Hertzig, A. E. Gorbalenya, V. Campanacci, C. Cambillau, B. Canard, and J. Ziebuhr
Discovery of an RNA virus 3'->5' exoribonuclease that is critically involved in coronavirus RNA synthesis
PNAS, March 28, 2006; 103(13): 5108 - 5113.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.