Affinage

TREX2

Three prime repair exonuclease 2 · UniProt Q9BQ50

Length
236 aa
Mass
25.9 kDa
Annotated
2026-06-10
63 papers in source corpus 19 papers cited in narrative 19 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TREX2 is a mammalian homodimeric 3'→5' DNA exonuclease of the DnaQ/RNase T family that trims 3' ends of duplex DNA and safeguards genome stability (PMID:10391904, PMID:11279105, PMID:15661738). The enzyme degrades DNA but not single-stranded RNA or RNA-DNA duplexes, and kinetic analysis defines it as a non-processive nuclease in which DNA binding is the rate-limiting step (PMID:10391904, PMID:11279105, PMID:18534978). Crystal structures place the two active sites at opposite outer edges of the dimer, with three arginine residues on flexible loops mediating DNA binding independently of catalysis; DNA engagement induces an active-site conformational change in both protomers even when only one binds substrate, providing the structural basis for cooperative DNA binding and inter-protomer communication during catalysis (PMID:15661738, PMID:18534978, PMID:19321497). Substrate recognition requires a long double-stranded region, with a Leu-Pro-Asn cluster stacking against the 5' terminus to position the 3' overhang for precise trimming, and the product complex explains its non-processive behavior (PMID:30357414). TREX2 physically associates with DNA polymerase delta to enhance replication fidelity under error-prone conditions (PMID:12806015), and it suppresses spontaneous double-strand breaks and chromosomal instability in a manner requiring its catalytic and DNA-binding activities, while an additional non-catalytic activity is needed to prevent Robertsonian translocations (PMID:17909011, PMID:19094998, PMID:21546543). TREX2 participates in the RAD18/UBC13-mediated PCNA-ubiquitination DNA damage tolerance pathway, where its exonuclease activity drives mutagenesis—particularly in mismatch-repair-deficient cells—whereas a non-catalytic function protects stalled replication forks from nascent strand degradation (PMID:33357432, PMID:38175749). In stratified squamous epithelia, TREX2 is preferentially expressed in keratinocytes, is induced by UV, and promotes apoptosis and DNA fragment degradation during genotoxic stress and cornification, with its loss reducing keratinocyte death and altering inflammatory responses in skin disease models (PMID:19654293, PMID:26090614, PMID:27365293, PMID:28928425).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 1999 High

    Established that TREX2 encodes a substrate-selective nuclease, answering what biochemical activity the gene product carries.

    Evidence Recombinant protein expressed in E. coli assayed against multiple substrate types in vitro

    PMID:10391904

    Open questions at the time
    • Cellular substrate not defined
    • No structural basis for DNA-only specificity
  2. 2001 High

    Defined TREX2 as a homodimer with rigorous kinetic parameters and a preference for 3' ends of partial duplex DNA, framing its likely DNA-end-processing role.

    Evidence Purified recombinant protein, steady-state kinetics, and heparin competition assays

    PMID:11279105

    Open questions at the time
    • In vivo substrate not identified
    • Functional partners unknown at this stage
  3. 2002 Medium

    Showed a physical and functional link to replicative polymerase delta, suggesting TREX2 contributes to replication fidelity rather than acting in isolation.

    Evidence Co-purification from calf thymus with M13mp2 forward-mutation and reversion fidelity assays

    PMID:12806015

    Open questions at the time
    • Single co-purification, no reciprocal validation
    • Direct binding interface undefined
    • Stoichiometry of complex unknown
  4. 2005 High

    Resolved the dimeric architecture and separated DNA-binding (arginine loops) from catalytic residues, distinguishing the two functions structurally.

    Evidence X-ray crystallography with site-directed mutagenesis and DNA binding assays

    PMID:15661738

    Open questions at the time
    • Apo structure only, no DNA-bound state
    • Mechanism of inter-active-site coordination unresolved
  5. 2007 Medium

    Linked TREX2 dysregulation to chromosomal rearrangement, showing cisplatin depletes TREX2 and that its loss drives Robertsonian translocations and reduced proliferation.

    Evidence Gene-targeted mouse ES cells, cisplatin/MMC chemical epistasis, and cytogenetic metaphase analysis

    PMID:17909011

    Open questions at the time
    • Mechanism linking depletion to translocations unclear
    • Single lab
  6. 2007 Medium

    Integrated dimerization, DNA binding, and catalysis as coupled functions and located TREX2 to a punctate nuclear pattern with cell-cycle regulation.

    Evidence Site-directed mutagenesis, immunofluorescence, siRNA knockdown, and cell cycle analysis

    PMID:17426129

    Open questions at the time
    • Nuclear puncta identity undefined
    • Mechanism of G2/M downregulation unknown
  7. 2008 Medium

    Demonstrated catalytic activity is required to suppress spontaneous DSBs while a separate activity prevents translocations, revealing TREX2 has more than one genome-protective function.

    Evidence Cre-mediated knock-in of H188A and R167A mutants in trex2-null ES cells with metaphase analysis

    PMID:19094998

    Open questions at the time
    • Nature of the additional non-catalytic activity unidentified
    • Single lab
  8. 2008 High

    Established inter-protomer communication and cooperative DNA binding as the kinetic mechanism of the dimer, with DNA binding rate-limiting.

    Evidence Steady-state and single-turnover kinetics, equilibrium binding, and heterodimer functional analysis

    PMID:18534978

    Open questions at the time
    • Structural basis of cross-protomer signaling not yet visualized
    • Physiological relevance of cooperativity untested in cells
  9. 2009 High

    Provided the structural mechanism for inter-protomer communication: DNA binding by one monomer reorders both active sites.

    Evidence X-ray crystallography of a TREX2–ssDNA complex

    PMID:19321497

    Open questions at the time
    • ssDNA complex only; duplex engagement not captured here
    • Catalytic cycle intermediates not resolved
  10. 2009 Medium

    Connected TREX2 to keratinocyte biology in vivo, showing its loss increases skin carcinogenesis susceptibility via reduced genotoxic-stress apoptosis.

    Evidence TREX2-null mice with DMBA carcinogenesis and TUNEL apoptosis assays

    PMID:19654293

    Open questions at the time
    • Molecular link between TREX2 and apoptosis undefined
    • Tissue-restricted role mechanism unknown
  11. 2011 Medium

    Clarified that TREX2 suppresses spontaneous chromosome breakage but is not a core DSB-repair factor, refining its place relative to HR and NHEJ.

    Evidence Metaphase analysis, SCE assays, I-SceI DSB repair reporter, and camptothecin/γ-radiation sensitivity assays

    PMID:21546543

    Open questions at the time
    • Basis of reduced SCE unexplained
    • Mechanism by which deletion enhances DSB repair unclear
  12. 2015 Medium

    Placed TREX2 at sites of DNA damage in keratinocytes through interaction with γH2AX, linking it to DNA repair and apoptotic progression after UV.

    Evidence TREX2 knockout mice, co-IP with γH2AX, immunofluorescence, and cytokine measurement after UVB

    PMID:26090614

    Open questions at the time
    • Direct vs indirect γH2AX association unresolved
    • Recruitment mechanism to micronuclei unknown
  13. 2016 Medium

    Extended TREX2's keratinocyte role to inflammatory skin disease, showing its loss attenuates psoriasis-like inflammation and shifts the differentiation/inflammation transcriptional program.

    Evidence Trex2 knockout mice in imiquimod/IL-23 psoriasis models with transcriptomics and immunofluorescence

    PMID:27365293

    Open questions at the time
    • Cell-autonomous vs non-autonomous contributions not fully separated
    • Mechanism linking DNA processing to immune gene expression undefined
  14. 2017 Medium

    Defined a redundant DNA-clearing role with DNase1L2 during cornification and showed keratinocytes tolerate retained DNA without DNA-sensor activation.

    Evidence Single and double knockout mice with histological/molecular analysis of tongue epithelium and qPCR of DNA-sensing genes

    PMID:28928425

    Open questions at the time
    • Substrate/structure of retained DNA fragments uncharacterized
    • Why DNA sensors stay silent mechanistically unexplained
  15. 2018 High

    Provided a comprehensive structural mechanism for substrate selection and non-processivity through multiple substrate and product complexes.

    Evidence Four crystal structures (apo, two dsDNA, post-catalytic product) with structural analysis

    PMID:30357414

    Open questions at the time
    • Dynamics of product release not directly observed
    • Coupling of structural states to dimer cooperativity not fully linked
  16. 2020 Medium

    Embedded TREX2 in the RAD18/UBC13/PCNA damage-tolerance pathway and separated a mutagenic catalytic role from a non-catalytic fork-protection role.

    Evidence Genetic deletion/mutagenesis in mouse and human cells, DNA fiber assays, mutation frequency, and co-IP for UBC13/PCNA ubiquitination

    PMID:33357432

    Open questions at the time
    • Mechanism of TREX2-driven PCNA ubiquitination undefined
    • How catalytic and non-catalytic functions are partitioned unclear
    • Single lab
  17. 2024 Medium

    Identified TREX2 as the dominant source of spontaneous mutations in MMR-deficient cells, dependent on both nuclease and DNA-binding activities.

    Evidence TREX2 knockout in MMR-deficient mouse and human cells with mutation assays, DNA fiber assays, and genetic epistasis

    PMID:38175749

    Open questions at the time
    • Substrate generating these mutations not directly identified
    • Relationship to fork-stall phenotype not fully mechanistic
  18. 2025 Medium

    Expanded the substrate repertoire to 3'-DNA-peptide cross-links from abasic sites, indicating a role in clearing repair-blocking adducts.

    Evidence In vitro enzymatic repair assay with chemically synthesized 3'-histone-DPC substrates

    PMID:41257340

    Open questions at the time
    • In vivo relevance not demonstrated
    • Single lab, single study
    • Synthetic adducts may not fully recapitulate physiological DPCs

Open questions

Synthesis pass · forward-looking unresolved questions
  • The identity of the additional non-catalytic biochemical activity that suppresses translocations and protects replication forks, and the molecular mechanism by which TREX2 promotes PCNA ubiquitination, remain unresolved.
  • Non-catalytic activity unidentified
  • Structural basis of UBC13/PCNA engagement unknown
  • How nuclease and scaffolding roles are coordinated in vivo unclear

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003677 DNA binding 4 GO:0140097 catalytic activity, acting on DNA 4 GO:0016787 hydrolase activity 3
Localization
GO:0005634 nucleus 2
Pathway
R-HSA-5357801 Programmed Cell Death 3 R-HSA-69306 DNA Replication 3 R-HSA-73894 DNA Repair 3
Partners
H2AXPCNAPOLBPOLD1UBC13

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 TREX2 encodes a mammalian 3'→5' exonuclease; recombinant TREX2 expressed in E. coli is an active 3'→5' exonuclease that degrades DNA but shows no activity on single-stranded RNA or RNA-DNA partial duplexes. Recombinant protein expression in E. coli; in vitro exonuclease activity assay with multiple substrate types The Journal of biological chemistry High 10391904
2001 TREX2 forms homodimers and exhibits robust 3'→5' exonuclease activity; steady-state kinetics show apparent kcat ~16 s⁻¹ and KM ~190 nM for single-stranded oligonucleotides; substrate preference analysis indicates the enzyme favors processing 3' ends of partial duplex DNAs. Recombinant protein purification from E. coli; steady-state kinetic analysis; exonuclease competition assay with heparin The Journal of biological chemistry High 11279105
2005 Crystal structure of human TREX2 reveals a dimeric 3'-deoxyribonuclease with active sites at opposite outer edges; three arginine residues on flexible loops adjacent to each active site mediate DNA binding (mutation to alanine reduces DNA binding ~100-fold with no effect on catalysis); catalytic residues overlay with bacterial DnaQ family, and their mutation reduces activity ~10⁵-fold confirming their catalytic role. X-ray crystallography; site-directed mutagenesis; DNA binding assays The Journal of biological chemistry High 15661738
2002 TREX2 physically associates with DNA polymerase delta (pol δ) purified from calf thymus under detergent conditions; this association increases the exonuclease-to-polymerase ratio ~20-fold and improves pol δ fidelity 4–5-fold under error-prone conditions, without affecting fidelity under balanced dNTP conditions. Co-purification from calf thymus extracts; M13mp2 forward mutation assay; M13mp2T90 reversion assay TheScientificWorldJournal Medium 12806015
2007 Endogenous TREX2 is predominantly expressed as a ~30 kDa protein (not 26 kDa), consistent with longer isoforms; site-directed mutagenesis shows that homodimerization, DNA binding, and catalytic activity are distinct but integrated functions — mutations impairing dimerization reduce both DNA binding and exonuclease activity, while exonuclease domain mutations diminish DNA binding but DNA-binding domain mutations do not impair catalysis; nuclear TREX2 displays a punctate staining pattern and is downregulated during G2/M; TREX2 knockdown reduces cell proliferation. Site-directed mutagenesis; immunofluorescence; siRNA knockdown; cell cycle analysis; immunoblotting Nucleic acids research Medium 17426129
2008 Steady-state and single-turnover kinetics, together with equilibrium DNA binding, demonstrate cooperative DNA binding within the TREX2 dimer and coordinated catalysis between active sites; mobile loops provide the primary DNA binding contribution; heterodimer experiments show that a catalytic defect (H188A) in one protomer reduces activity in the opposing protomer ~7-fold, confirming inter-protomer communication; DNA binding is the rate-limiting step in TREX2 catalysis. Steady-state kinetics; single-turnover kinetics; equilibrium DNA binding; heterodimer preparation and analysis The Journal of biological chemistry High 18534978
2009 Crystal structure of TREX2 in complex with single-stranded DNA reveals that DNA binding induces an active-site conformational change, including ordering of active site residues and a shift of an active site helix; even when only one monomer binds DNA, both monomers undergo the structural rearrangement, providing a structural basis for inter-protomer communication. X-ray crystallography of TREX2–ssDNA complex Nucleic acids research High 19321497
2007 Cisplatin exposure depletes TREX2 protein in human cancer-derived cells; deletion of TREX2 in mouse embryonic stem cells causes reduced proliferation and Robertsonian translocations (RbTs); cisplatin-treated ES cells also exhibit RbTs, whereas mitomycin C (which does not deplete TREX2) does not cause RbTs, indicating TREX2 depletion specifically underlies cisplatin-associated chromosomal rearrangements. Gene targeting in mouse ES cells; cisplatin/MMC treatment; metaphase spread analysis; cytogenetics Cancer research Medium 17909011
2008 Using trex2-null mouse ES cells re-expressing H188A (exonuclease-dead) or R167A (DNA-binding-impaired) TREX2, catalytic activity is required to suppress spontaneous double-strand breaks and chromosomal fragments; neither the exonuclease nor the DNA-binding domains are sufficient to suppress Robertsonian translocations, suggesting an additional biochemical activity of TREX2. Cre-mediated knock-in; metaphase spread analysis; site-directed mutagenesis Mutation research Medium 19094998
2009 TREX2-null mice are viable but show increased susceptibility to DMBA-induced skin carcinogenesis; the phenotype correlates with reduced apoptosis in keratinocytes following genotoxic stress; TREX2 expression is preferential in stratified squamous epithelial tissues/keratinocytes. Knockout mouse generation; DMBA skin carcinogenesis protocol; TUNEL apoptosis assays Cancer research Medium 19654293
2011 Trex2-null and H188A (catalytic-dead) cells exhibit spontaneous broken chromosomes; trex2-null cells show reduced spontaneous sister chromatid exchanges (SCEs) that are not due to a defect in HR-mediated crossing over; Trex2 deletion enhances repair of an I-SceI-induced DSB by both HDR and NHEJ without affecting pathway choice; Trex2-altered cells are not hypersensitive to camptothecin or γ-radiation, indicating Trex2 does not enable DSB repair per se. Metaphase spread analysis; sister chromatid exchange assay; I-SceI DSB repair assay; camptothecin and γ-radiation sensitivity assays Genetics Medium 21546543
2015 TREX2 is upregulated by UV exposure in keratinocytes; TREX2 deficiency leads to aberrant DNA damage removal and reduced inflammation after UVB; TREX2 is recruited to low-density nuclear chromatin and micronuclei where it physically interacts with phosphorylated H2AX; TREX2 promotes DNA repair and passage to late apoptotic stages in UV-treated keratinocytes. TREX2 knockout mice; UVB carcinogenesis protocol; co-immunoprecipitation with γH2AX; immunofluorescence; cytokine measurement Oncotarget Medium 26090614
2016 Trex2 is recruited to fragmented chromatin in keratinocytes during psoriasis; Trex2 deficiency attenuates imiquimod-induced psoriasis-like inflammation and reduces keratinocyte death; Trex2 loss decreases immune/inflammatory gene expression while increasing skin differentiation genes; keratinocyte apoptosis/enucleation is reduced in Trex2-null mice through both cell-autonomous and non-cell-autonomous mechanisms. Trex2 knockout mice; imiquimod/IL-23 psoriasis models; transcriptome analysis; immunofluorescence The Journal of investigative dermatology Medium 27365293
2017 Deletion of both DNase1L2 and Trex2 causes massive accumulation of DNA fragments throughout cornified layers of the tongue epithelium, whereas single knockouts show partial defects; Trex2 loss alone causes cytoplasmic DNA fragment accumulation in lingual cornifying keratinocytes; keratinocytes express very low levels of DNA-sensor genes (Tlr9, Aim2, Tmem173) and do not induce inflammatory DNA-response genes despite aberrant DNA retention. Single and double knockout mice; histological and molecular analysis of tongue epithelium; qPCR for DNA-sensing genes Scientific reports Medium 28928425
2018 Four crystal structures of TREX2 (apo, two dsDNA complexes, and a post-catalytic product complex) reveal that TREX2 uses a Leu20-Pro21-Asn22 cluster to stack with the 5'-terminal of dsDNA for precise 3'-overhang trimming; an α-helix-loop region specifically contacts the non-scissile strand; a long double-stranded region is required for TREX2 binding; the non-processive property is explained structurally by the product-complex structure. X-ray crystallography (four structures); structural analysis of dsDNA binding and product release Nucleic acids research High 30357414
2020 TREX2 participates in DNA damage tolerance (DDT) via RAD18/UBC13-mediated PCNA ubiquitination; in RAD51K133A cells, TREX2 H188A (catalytic-dead) reduces spontaneous mutations and RF stalls, while TREX2 exonuclease activity drives mutagenesis; deleting TREX2 in PARP1- or FANCB-deficient cells increases nascent strand degradation rescued by TREX2H188A (non-catalytic), implicating TREX2 in RF protection independent of catalysis; TREX2H188A associates with UBC13 and ubiquitinates PCNA. Genetic deletion and mutagenesis in mouse/human cells; DNA fiber assay; mutation frequency assay; Co-IP for UBC13 and PCNA ubiquitination Cell reports Medium 33357432
2024 TREX2 deletion reduces spontaneous and genotoxin-induced mutations; TREX2 generates most spontaneous mutations in MMR-deficient cells; mutagenesis depends on both TREX2 nuclease activity and DNA-binding activity; RAD18 deletion also reduces mutations in MMR-deficient cells; simultaneous loss of MMR and TREX2 additively increases RF stalls while decreasing DNA breaks. TREX2 knockout in MMR-deficient mouse and human cells; mutation frequency assays; DNA fiber assay; genetic epistasis Cell reports Medium 38175749
2010 Recombinant TREX2 forms a complex with DNA polymerase beta in vitro (gel filtration), and the presence of TREX2 increases DNA polymerase beta activity approximately 4-fold; direct binding confirmed by immunodot and Western blot on nitrocellulose-immobilized proteins. Gel filtration; immunodot; Western blot binding assay Izvestiia Akademii nauk. Seriia biologicheskaia Low 21077363
2025 TREX2 (and APE2) can repair 3'-DNA-peptide cross-links (3'-histone-DPCs) derived from abasic sites in vitro; these are chemically synthesized adducts resembling proteolyzed Schiff base 3'-histone-DPCs that block DNA repair synthesis. In vitro enzymatic repair assay with chemically synthesized 3'-DPC substrates Chemical research in toxicology Medium 41257340

Source papers

Stage 0 corpus · 63 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 BRCA2 prevents R-loop accumulation and associates with TREX-2 mRNA export factor PCID2. Nature 441 24896180
1999 Identification and expression of the TREX1 and TREX2 cDNA sequences encoding mammalian 3'-->5' exonucleases. The Journal of biological chemistry 242 10391904
2001 Excision of 3' termini by the Trex1 and TREX2 3'-->5' exonucleases. Characterization of the recombinant proteins. The Journal of biological chemistry 139 11279105
2012 Functional and structural characterization of the mammalian TREX-2 complex that links transcription with nuclear messenger RNA export. Nucleic acids research 120 22307388
2013 The human TREX-2 complex is stably associated with the nuclear pore basket. Journal of cell science 116 23591820
2020 Nucleoporin TPR is an integral component of the TREX-2 mRNA export pathway. Nature communications 100 32917881
2012 Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex. Nature structural & molecular biology 98 22343721
2008 Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2. Genes & development 86 18923079
2014 Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export. Nucleic acids research 66 24705649
2001 Structure and expression of the TREX1 and TREX2 3' --> 5' exonuclease genes. The Journal of biological chemistry 64 11278605
2005 The human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis. The Journal of biological chemistry 52 15661738
2007 Biochemical and cellular characteristics of the 3' -> 5' exonuclease TREX2. Nucleic acids research 34 17426129
2009 Increased Susceptibility to Skin Carcinogenesis in TREX2 Knockout Mice. Cancer research 28 19654293
2015 Structural Characterization of the Chaetomium thermophilum TREX-2 Complex and its Interaction with the mRNA Nuclear Export Factor Mex67:Mtr2. Structure (London, England : 1993) 27 26051714
2019 Structure and Function of the TREX-2 Complex. Sub-cellular biochemistry 26 31939161
2023 Influenza virus mRNAs encode determinants for nuclear export via the cellular TREX-2 complex. Nature communications 24 37085480
2018 Transcription and mRNA export machineries SAGA and TREX-2 maintain monoubiquitinated H2B balance required for DNA repair. The Journal of cell biology 24 30054449
2016 The Exonuclease Trex2 Shapes Psoriatic Phenotype. The Journal of investigative dermatology 19 27365293
2007 Cisplatin depletes TREX2 and causes Robertsonian translocations as seen in TREX2 knockout cells. Cancer research 19 17909011
2018 Structural insights into the duplex DNA processing of TREX2. Nucleic acids research 18 30357414
2015 Multifaceted role of TREX2 in the skin defense against UV-induced skin carcinogenesis. Oncotarget 17 26090614
2002 The TREX2 3'-->5' exonuclease physically interacts with DNA polymerase delta and increases its accuracy. TheScientificWorldJournal 17 12806015
2019 Measuring TREX1 and TREX2 exonuclease activities. Methods in enzymology 16 31455522
2017 Double deficiency of Trex2 and DNase1L2 nucleases leads to accumulation of DNA in lingual cornifying keratinocytes without activating inflammatory responses. Scientific reports 16 28928425
2008 Cooperative DNA binding and communication across the dimer interface in the TREX2 3' --> 5'-exonuclease. The Journal of biological chemistry 16 18534978
2025 Structures and mRNP remodeling mechanism of the TREX-2 complex. Structure (London, England : 1993) 15 39862860
2011 Trex2 enables spontaneous sister chromatid exchanges without facilitating DNA double-strand break repair. Genetics 15 21546543
2009 DNA binding induces active site conformational change in the human TREX2 3'-exonuclease. Nucleic acids research 15 19321497
2008 TREX2 exonuclease defective cells exhibit double-strand breaks and chromosomal fragments but not Robertsonian translocations. Mutation research 15 19094998
2025 Structural mechanism of DDX39B regulation by human TREX-2 and a related complex in mRNP remodeling. Nature communications 14 40595470
2021 PCID2, a subunit of the Drosophila TREX-2 nuclear export complex, is essential for both mRNA nuclear export and its subsequent cytoplasmic trafficking. RNA biology 14 33602059
2017 Structure of the Sac3 RNA-binding M-region in the Saccharomyces cerevisiae TREX-2 complex. Nucleic acids research 14 28334829
2016 Mediator and TREX-2: Emerging links between transcription initiation and mRNA export. Nucleus (Austin, Tex.) 14 27028218
2013 Human TREX2 components PCID2 and centrin 2, but not ENY2, have distinct functions in protein export and co-localize to the centrosome. Experimental cell research 13 24291146
2013 A novel role for Sem1 and TREX-2 in transcription involves their impact on recruitment and H2B deubiquitylation activity of SAGA. Nucleic acids research 12 23599000
2020 TREX2 Exonuclease Causes Spontaneous Mutations and Stress-Induced Replication Fork Defects in Cells Expressing RAD51K133A. Cell reports 10 33357432
2014 Unveiling novel interactions of histone chaperone Asf1 linked to TREX-2 factors Sus1 and Thp1. Nucleus (Austin, Tex.) 10 24824343
2022 Sus1 maintains a normal lifespan through regulation of TREX-2 complex-mediated mRNA export. Aging 8 35771153
2016 The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. Journal of structural biology 8 27422657
2024 Efficient gene disruption in polyploid genome by Cas9-Trex2 fusion protein. Journal of integrative plant biology 6 39451161
2023 TREX2 enables efficient genome disruption mediated by paired CRISPR-Cas9 nickases that generate 3'-overhanging ends. Molecular therapy. Nucleic acids 5 38028195
2023 Interaction of mRNA with the C-Terminal Domain of PCID2, a Subunit of the TREX-2 Complex, Is Required for Its Export from the Nucleus to the Cytoplasm in Drosophila melanogaster. Doklady. Biochemistry and biophysics 5 38066318
2023 PCID2 Subunit of the Drosophila TREX-2 Complex Has Two RNA-Binding Regions. Current issues in molecular biology 4 37504273
2015 1.25 Å resolution structure of an RNA 20-mer that binds to the TREX2 complex. Acta crystallographica. Section F, Structural biology communications 4 26457524
2024 TREX2 deficiency suppresses spontaneous and genotoxin-associated mutagenesis. Cell reports 3 38175749
2021 Study of the Interaction between Xmas-2, the Main Protein of TREX-2 mRNA Export Complex, and the Orc3 Protein, a Subunit of ORC Complex of D. melanogaster. Doklady. Biochemistry and biophysics 3 33689068
2021 Trex2 responds to damaged replication forks in diverse ways. Molecular & cellular oncology 3 33860084
2024 Tumorigenesis Caused by Aberrant Expression of GANP, a Central Component in the Mammalian TREX-2 Complex-Lessons from Transcription-Coupled DNA Damages. International journal of molecular sciences 2 39769375
2025 TREX-2 mRNA Export Complex Interacts with HLB Component FLASH and Is Recruited to Processed Histone mRNAs. Doklady. Biochemistry and biophysics 1 41083635
2024 Carcinogenesis caused by transcription-coupled DNA damage through GANP and other components of the TREX-2 complex. Pathology international 1 38411330
2024 [Drosophila melanogaster Paip2 Binds ENY2 and Interacts with the TREX-2 Complex in Histone mRNP Particles]. Molekuliarnaia biologiia 1 39707855
2020 The Xmas-2 Homologues, the Main Component of the TREX-2 mRNA Export Complex. Doklady. Biochemistry and biophysics 1 33368044
2016 [Interactions of the TREX-2 complex with mRNP particle of β-tubulin 56D gene]. Molekuliarnaia biologiia 1 28064320
2010 [Investigation of the interaction of repair DNA polymerase beta and autonomous 3' --> 5'-exonucleases TREX1 and TREX2]. Izvestiia Akademii nauk. Seriia biologicheskaia 1 21077363
2026 Molecular insights into mRNA export regulation by the human TREX-2 complex. Nature communications 0 41748650
2026 TREX2 component PCID2 scaffolds alternative SAC3-based subcomplexes with distinct RNA processing and export function. bioRxiv : the preprint server for biology 0 42039562
2026 Optimized tRNA processing and TREX2-SpCas9 fusion enable high-efficiency multiplex genome editing in plants. Plant communications 0 42163455
2025 Nup153 and TPR/Megator Interact with TREX-2 Subunits and Are Essential for TREX-2-Dependent Nuclear Export of hsp70 mRNA in Drosophila. International journal of molecular sciences 0 40943515
2025 Interdomain Interactions of the PCID2 Protein, One of the Subunits of the TREX-2 mRNA Export Complex in Drosophila melanogaster. Doklady. Biochemistry and biophysics 0 41083629
2025 Two RNA-Binding Regions of PCID2, a Subunit of the TREX-2 mRNA Nuclear Export Complex, Competitively Interact with the 3' Noncoding Region of ras2 mRNA. Doklady. Biochemistry and biophysics 0 41083631
2025 Human APE2 and TREX2 Repair 3'-DNA-Peptide Cross-links Derived from Abasic Sites. Chemical research in toxicology 0 41257340
2024 Xmas-2 Protein, the Core Protein of the TREX-2 mRNA Export Complex, Does not Determine the Specificity of ras2 mRNA Binding by the Complex. Doklady. Biochemistry and biophysics 0 39196529
2023 The Human TREX-2 Complex Interacts with Subunits of the ORC Complex. Doklady. Biochemistry and biophysics 0 38066323

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