This gene encodes the major 3' to 5' DNA exonuclease in human cells. The protein is a non-processive exonuclease that appears to provide proofreading for checkpoint signaling after DNA damage in response to oxidative stress and apoptosis. It is ubiquitously expressed. Trex1 binds to single-stranded DNA coated with replication protein A found at sites of DNA damage, and recruits the ataxia telangiectasia and Rad3 related protein (ATR) checkpoint kinase. This gene uses two different open reading frames. The upstream ORF encodes proteins which interact with ATR and localize to the intranuclear foci induced by DNA damage. The downstream ORF encodes proteins with 3' to 5' exonuclease activity and may be a subunit of human DNA polymerase III.
Mutations in this gene result in Aicardi-Goutieres syndrome, chilblain lupus, and Cree encephalitis. TREX1 antibody will not cross-react with the related protein TREX2. It is also a component of the SET complex, and acts to rapidly degrade 3' ends of nicked DNA during granzyme A-mediated cell death. A recent review by Hasan et al highlights the host mechanisms of HIV-1 infection and viral immune evasion with respect to Trex1’s role as a safeguard against DNA sensing (1). Autoimmune disease investigators review the role of rare mutational Trex1 variants in SLE and Sjogren's syndrome (SS) (2). The Trex1 antibody was used by Christmann’s group from the Mainz University Medical Center to analyze cell response to genotoxic stress (3). Their data demonstrates that upon UV light treatment, Trex1 is induced and in turn induces AP-1.
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