JBC PeproTech; Our Business is Cytokines!

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


     

A more recent version of this article appeared on May 11, 2001
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
276/20/17022    most recent
M100623200v1
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 Mazur, D. J.
Right arrow Articles by Perrino, F. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mazur, D. J.
Right arrow Articles by Perrino, F. W.
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 March 6, 2001
J. Biol. Chem, 10.1074/jbc.M100623200
Submitted on January 23, 2001
Revised on March 6, 2001
Accepted on March 5, 2001

Excision of 3' termini by the Trex1 and TREX2 3'-5' exonucleases: characterization of the recombinant proteins

Dan J. Mazur and Fred W. Perrino

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

Corresponding Author: fperrino{at}wfubmc.edu

The excision of nucleotides from DNA 3' termini is an important step in DNA replication, repair, and recombination pathways to generate correctly basepaired termini for subsequent processing. The mammalian TREX1 and TREX2 proteins contain potent 3'-5' exonucleases capable of functioning in this capacity. To study the activities of these exonucleases we have developed strategies to express and purify the recombinant mouse Trex1 and human TREX2 proteins in Escherichia coli in quantities sufficient for biochemical characterization. The Trex1 and TREX2 proteins are homodimers that exhibit robust 3' excision activities with very similar preferred reaction conditions and preferences for specific DNA substrates. In a steady state kinetic analysis oligonucleotide substrates were used to measure 3' nucleotide excision by Trex1 and TREX2. The Michaelis constants derived from these data indicate similar apparent kcat values of 22 s-1 for Trex1 and 16 s-1 for TREX2 using single-stranded oligonucleotides. The apparent KM values of 19 nM for Trex1 and 190 nM for TREX2 suggest relatively high affinities for DNA for both Trex1 and TREX2. An exonuclease competition assay was designed using heparin as a nonsubstrate inhibitor with a series of partial duplex DNAs to delineate the substrate structure preferences for 3' nucleotide excision by Trex1 and TREX2. The catalytic properties of the TREX proteins suggest roles for these enzymes in the 3' end-trimming processes necessary for producing correctly basepaired 3' termini.


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
 Cancer Res.Home page
M.-J. Chen, L. C. Dumitrache, D. Wangsa, S.-M. Ma, H. Padilla-Nash, T. Ried, and P. Hasty
Cisplatin Depletes TREX2 and Causes Robertsonian Translocations as Seen in TREX2 Knockout Cells
Cancer Res., October 1, 2007; 67(19): 9077 - 9083.
[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
 Cancer Res.Home page
Z.-Y. Liao, O. Sordet, H.-L. Zhang, G. Kohlhagen, S. Antony, W. H. Gmeiner, and Y. Pommier
A Novel Polypyrimidine Antitumor Agent FdUMP[10] Induces Thymineless Death with Topoisomerase I-DNA Complexes
Cancer Res., June 1, 2005; 65(11): 4844 - 4851.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. W. Perrino, S. Harvey, S. McMillin, and T. Hollis
The Human TREX2 3' -> 5'-Exonuclease Structure Suggests a Mechanism for Efficient Nonprocessive DNA Catalysis
J. Biol. Chem., April 15, 2005; 280(15): 15212 - 15218.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
D.-H. Yang, J. G. de Jong, A. Makhmoudova, B. M. Arif, and P. J. Krell
Choristoneura fumiferana nucleopolyhedrovirus encodes a functional 3'-5' exonuclease
J. Gen. Virol., December 1, 2004; 85(12): 3569 - 3573.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
J. Bentley, C. P. Diggle, P. Harnden, M. A. Knowles, and A. E. Kiltie
DNA double strand break repair in human bladder cancer is error prone and involves microhomology-associated end-joining
Nucleic Acids Res., October 5, 2004; 32(17): 5249 - 5259.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
J. M. Slack and M. Shapiro
Anticarsia gemmatalis multicapsid nucleopolyhedrovirus v-trex gene encodes a functional 3' to 5' exonuclease
J. Gen. Virol., October 1, 2004; 85(10): 2863 - 2871.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
M. Morita, G. Stamp, P. Robins, A. Dulic, I. Rosewell, G. Hrivnak, G. Daly, T. Lindahl, and D. E. Barnes
Gene-Targeted Mice Lacking the Trex1 (DNase III) 3'->5' DNA Exonuclease Develop Inflammatory Myocarditis
Mol. Cell. Biol., August 1, 2004; 24(15): 6719 - 6727.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Ma, J. R. McCorkle, and D. M. Kaetzel
The Metastasis Suppressor NM23-H1 Possesses 3'-5' Exonuclease Activity
J. Biol. Chem., April 23, 2004; 279(17): 18073 - 18084.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
J. M. Slack, B. M. Ribeiro, and M. L. de Souza
The gp64 locus of Anticarsia gemmatalis multicapsid nucleopolyhedrovirus contains a 3' repair exonuclease homologue and lacks v-cath and ChiA genes
J. Gen. Virol., January 1, 2004; 85(1): 211 - 219.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
I. Kuraoka, P. Robins, C. Masutani, F. Hanaoka, D. Gasparutto, J. Cadet, R. D. Wood, and T. Lindahl
Oxygen Free Radical Damage to DNA. TRANSLESION SYNTHESIS BY HUMAN DNA POLYMERASE eta AND RESISTANCE TO EXONUCLEASE ACTION AT CYCLOPURINE DEOXYNUCLEOSIDE RESIDUES
J. Biol. Chem., December 21, 2001; 276(52): 49283 - 49288.
[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.