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Three prime repair exonuclease 2

This gene encodes a protein with 3' exonuclease activity. Enzymes with this activity are involved in DNA replication, repair, and recombination. Similarity to an E. coli protein suggests that this enzyme may be a subunit of DNA polymerase III, which does not have intrinsic exonuclease activity. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, POLYMERASE, ss2, DNase I, V1a
Papers on TREX2
Detection of treatment-resistant infectious HIV after genome-directed antiviral endonuclease therapy.
Jerome et al., Seattle, United States. In Antiviral Res, Jan 2016
While testing the activity of HIV pol-specific zinc finger nucleases (ZFNs) alone or in combination with three prime repair exonuclease 2 (Trex2), we identified a treatment-resistant and infectious mutant virus that was derived from a ZFN-mediated disruption of reverse transcriptase (RT).
1.25 Å resolution structure of an RNA 20-mer that binds to the TREX2 complex.
Stewart et al., Cambridge, United Kingdom. In Acta Crystallogr Sect F Struct Biol Commun, Oct 2015
The 1.25 Å resolution H32:R crystal structure of a 20 nt ribonucleotide that binds to the TREX-2 complex with high affinity shows a double-stranded RNA duplex arranged along a crystallographic 31 axis in which the antiparallel chains overlap by 18 nucleotides and are related by a crystallographic twofold axis.
Multifaceted role of TREX2 in the skin defense against UV-induced skin carcinogenesis.
Soler et al., Barcelona, Spain. In Oncotarget, Oct 2015
TREX2 is a 3'-DNA exonuclease specifically expressed in keratinocytes.
Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export.
Stewart et al., Cambridge, United Kingdom. In Nucleic Acids Res, 2014
The conserved Sac3:Thp1:Sem1:Sus1:Cdc31 (TREX2) complex binds to nuclear pore complexes (NPCs) and, in addition to integrating mRNA nuclear export with preceding steps in the gene expression pathway, facilitates re-positioning of highly regulated actively transcribing genes (such as GAL1) to NPCs.
Human TREX2 components PCID2 and centrin 2, but not ENY2, have distinct functions in protein export and co-localize to the centrosome.
Resendes et al., United States. In Exp Cell Res, 2014
TREX-2 is a five protein complex, conserved from yeast to humans, involved in linking mRNA transcription and export.
In vitro Inactivation of Latent HSV by Targeted Mutagenesis Using an HSV-specific Homing Endonuclease.
Jerome et al., Seattle, United States. In Mol Ther Nucleic Acids, 2013
Coexpression of the 3'-exonuclease Trex2 with HEs increased HE-mediated mutagenesis frequencies up to sixfold.
Two replication fork maintenance pathways fuse inverted repeats to rearrange chromosomes.
Hasty et al., San Antonio, United States. In Nature, 2013
Furthermore, TREX2 (a 3'→5' exonuclease) suppressed identical repeat fusion but enhanced mismatched repeat fusion, clearly separating these pathways.
Exome resequencing identifies potential tumor-suppressor genes that predispose to colorectal cancer.
Cheadle et al., Cardiff, United Kingdom. In Hum Mutat, 2013
We sought somatic mutations in the corresponding genes in the CRCs of the patients harboring the germline lesions and found biallelic inactivation of FANCM, LAMB4, PTCHD3, LAMC3, and TREX2, potentially implicating these genes as tumor suppressors.
mRNA export and gene expression: the SAGA-TREX-2 connection.
Rodríguez-Navarro et al., Valencia, Spain. In Biochim Biophys Acta, 2012
In this review, we focus on the functional coupling of gene transcription and mRNA export, and place particular emphasis on the relationship between the NPC-associated complex, TREX2, and the transcription co-activator, SAGA.
Correct end use during end joining of multiple chromosomal double strand breaks is influenced by repair protein RAD50, DNA-dependent protein kinase DNA-PKcs, and transcription context.
Stark et al., Duarte, United States. In J Biol Chem, 2012
To investigate the maintenance of correct end use, we examined repair of two tandem noncohesive DSBs generated by endonuclease I-SceI and the 3' nonprocessive exonuclease Trex2, which can be expressed as an I-SceI-Trex2 fusion.
Mechanisms and emerging functions of DNA degradation in the epidermis.
Tschachler et al., Vienna, Austria. In Front Biosci, 2011
Deoxyribonuclease (DNase)1L2 and TREX2 were identified as epidermis-specific DNases and DNase 2 was shown to be the predominant DNA-degrading enzyme on the surface of the skin.
I-SceI-based assays to examine distinct repair outcomes of mammalian chromosomal double strand breaks.
Stark et al., Duarte, United States. In Methods Mol Biol, 2011
The EJ5-GFP reporter can also be adapted to examine EJ of non-cohesive DSB ends, using co-expression of I-SceI with a non-processive 3' exonuclease (Trex2), which can cause partial degradation of the 4 nucleotide 3' cohesive overhangs generated by I-SceI.
Trex2 enables spontaneous sister chromatid exchanges without facilitating DNA double-strand break repair.
Hasty et al., San Antonio, United States. In Genetics, 2011
Trex2 does not enable DSB repair and prompt a new model that posits Trex2 suppresses the formation of broken chromosomes.
ATM limits incorrect end utilization during non-homologous end joining of multiple chromosome breaks.
Stark et al., Duarte, United States. In Plos Genet, 2010
These DSBs are processed into non-cohesive ends by the exonuclease Trex2, which leads to the formation of I-SceI-resistant EJ products during both Proximal-EJ and Distal-EJ.
Increased Susceptibility to Skin Carcinogenesis in TREX2 Knockout Mice.
Soler et al., l'Hospitalet de Llobregat, Spain. In Cancer Res, 2009
A tumor suppressor role for TREX2 in skin carcinogenesis through which it contributes to keratinocyte apoptosis under conditions of genotoxic stress.
DNA binding induces active site conformational change in the human TREX2 3'-exonuclease.
Hollis et al., Winston-Salem, United States. In Nucleic Acids Res, 2009
a model for DNA binding and 3' hydrolysis for the TREX2 dimer.
A tale of coupling, Sus1 function in transcription and mRNA export.
Rodríguez-Navarro et al., Valencia, Spain. In Rna Biol, 2009
The evolutionarily conserved export factor Sus1 plays a key role in coupling transcription activation with mRNA export as part of the nuclear pore associated complex TREX2 and the transcriptional coactivator SAGA.
TREX2 exonuclease defective cells exhibit double-strand breaks and chromosomal fragments but not Robertsonian translocations.
Hasty et al., San Antonio, United States. In Mutat Res, 2009
Trex2 deletion caused high levels of Robertsonian translocations (RbTs) showing Trex2 is important for chromosomal maintenance.
Cooperative DNA binding and communication across the dimer interface in the TREX2 3' --> 5'-exonuclease.
Hollis et al., Winston-Salem, United States. In J Biol Chem, 2008
analysis of cooperative DNA binding and communication across the dimer interface in the TREX2 3' --> 5'-exonuclease
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