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Nucleic Acids Research Advance Access originally published online on March 24, 2009
Nucleic Acids Research 2009 37(7):2411-2417; doi:10.1093/nar/gkp025
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Nucleic Acids Research, 2009, Vol. 37, No. 7 2411-2417
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

DNA binding induces active site conformational change in the human TREX2 3'-exonuclease

Udesh de Silva, Fred W. Perrino and Thomas Hollis*

Department of Biochemistry, Center for Structural Biology, Wake Forest University Health Sciences, Winston-Salem, NC 27157, USA

*To whom correspondence should be addressed. Tel: +1 336 716 0768; Fax: +1 336 7777 3242; Email: thollis{at}wfubmc.edu

Received September 29, 2008. Revised January 6, 2009. Accepted January 12, 2009.

The TREX enzymes process DNA as the major 3'->5' exonuclease activity in mammalian cells. TREX2 and TREX1 are members of the DnaQ family of exonucleases and utilize a two metal ion catalytic mechanism of hydrolysis. The structure of the dimeric TREX2 enzyme in complex with single-stranded DNA has revealed binding properties that are distinct from the TREX1 protein. The TREX2 protein undergoes a conformational change in the active site upon DNA binding including ordering of active site residues and a shift of an active site helix. Surprisingly, even when a single monomer binds DNA, both monomers in the dimer undergo the structural rearrangement. From this we have proposed a model for DNA binding and 3' hydrolysis for the TREX2 dimer. The structure also shows how TREX proteins potentially interact with double-stranded DNA and suggest features that might be involved in strand denaturation to provide a single-stranded substrate for the active site.


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