| 1999 |
PARP-2 is a damaged DNA-binding protein that catalyzes poly(ADP-ribose) polymer synthesis in a DNA-dependent manner, displays automodification properties, and is localized in the nucleus; it accounts for residual poly(ADP-ribose) synthesis in PARP-1-deficient cells. |
In vitro biochemical assay with purified recombinant PARP-2; nuclear localization by in vivo experiments |
The Journal of biological chemistry |
High |
10364231
|
| 2002 |
PARP-2 homo- and heterodimerizes with PARP-1 (interacting interfaces mapped and shown to be sites of reciprocal modification); PARP-2 interacts with XRCC1, DNA polymerase beta, and DNA ligase III; XRCC1 negatively regulates PARP-2 activity while being a polymer acceptor for PARP-2; PARP-2-deficient cells display delayed DNA strand break resealing after alkylating agent treatment, confirming a role in base excision repair. |
Co-immunoprecipitation/pull-down for interactions; interface mapping; PARP-2 knockout mouse model with MNU treatment; BER assay |
The Journal of biological chemistry |
High |
11948190
|
| 2003 |
PARP-2-deficient mouse embryonic fibroblasts show increased post-replicative genomic instability, G2/M accumulation, chromosome mis-segregation, and kinetochore defects after alkylating agent treatment; PARP-1/PARP-2 double-knockout mice die at gastrulation, demonstrating functional redundancy; specific female embryonic lethality in parp-1+/-parp-2-/- mutants is linked to X chromosome instability. |
Gene-targeted mouse knockout; metaphase cytogenetics; cell cycle analysis of MEFs |
The EMBO journal |
High |
12727891
|
| 2004 |
PARP-2 physically binds TRF2 with high affinity; the interaction requires the N-terminal domain of PARP-2 and the myb domain of TRF2; PARP activity negatively regulates TRF2 DNA-binding via covalent heteromodification of TRF2's dimerization domain and noncovalent binding of poly(ADP-ribose) to TRF2's myb domain; PARP-2-deficient cells show spontaneously increased chromosome breaks and telomere ends lacking TTAGGG repeats. |
Co-immunoprecipitation, pull-down assays, domain mapping, TRF2 ADP-ribosylation in vitro, PARP-2 KO cells analyzed for telomere integrity |
Molecular and cellular biology |
High |
14749375
|
| 2005 |
PARP-2 accumulates in the nucleolus and colocalizes with nucleophosmin/B23; PARP-2 interacts with B23 through its N-terminal DNA binding domain; a nucleolar localization signal within the PARP-2 N-terminal domain is required for nucleolar accumulation; PARP-1 and PARP-2 are delocalized from the nucleolus upon RNA polymerase I inhibition. |
Immunofluorescence/live imaging, co-immunoprecipitation, nuclear localization signal mutant analysis, RNA Pol I inhibition experiments |
Journal of cell science |
High |
15615785
|
| 2006 |
PARP-2 deficiency in mice causes a two-fold reduction in CD4+CD8+ double-positive thymocytes associated with decreased DP cell survival; PARP-2-deficient DP thymocytes show increased Noxa expression, reduced TCRα expression, and skewed TCRα repertoire; PARP-2 acts as a survival factor during TCRα recombination to prevent DNA damage-dependent apoptosis. |
PARP-2 knockout mouse model, flow cytometry, microarray gene expression analysis, T-cell repertoire analysis |
The EMBO journal |
High |
16946705
|
| 2006 |
PARP-2 interacts with TTF-1 (thyroid transcription factor 1) via the E domain of PARP-2 and the C-terminal domain of TTF-1; PARP-2 (and PARP-1) enhance the activity of the surfactant protein-B (Sftpb) promoter in vitro; PARP-2 is expressed in epithelial cells of fetal and adult lung at sites consistent with surfactant protein B expression. |
Co-immunoprecipitation, mass spectrometry identification of endogenous complex, domain mapping, promoter reporter assay |
The Journal of biological chemistry |
High |
16461352
|
| 2008 |
PARP-2 interacts with TIF1beta (KAP1) and HP1alpha directly and through HP1alpha; Parp-2 poly(ADP-ribosyl)ates HP1alpha selectively; Parp-2 and its enzymatic activity are required for relocation of TIF1beta to heterochromatic foci during primitive endodermal differentiation; both Parps control TIF1beta transcriptional activity. |
Co-immunoprecipitation, pull-down assays, shRNA knockdown, immunofluorescence/colocalization, in vitro PARylation assay |
FASEB journal |
High |
18676401
|
| 2008 |
PARP-2 is acetylated by histone acetyltransferases PCAF and GCN5L at lysines 36 and 37 in its nuclear localization signal; acetylation at K36/K37 reduces PARP-2 DNA binding and enzymatic activity; K36/K37 mutant PARP-2 shows reduced auto-mono-ADP-ribosylation. |
In vitro acetylation assay, site-directed mutagenesis, PARP activity assay, DNA binding assay |
The international journal of biochemistry & cell biology |
High |
18436469
|
| 2009 |
Parp1 facilitates alternative/microhomology-mediated end-joining during immunoglobulin class switch recombination, whereas Parp2 actively suppresses IgH/c-myc translocations; PARP enzymatic activity is induced in an AID-dependent manner during CSR; neither Parp1 nor Parp2 is required for CSR itself. |
Parp1 and Parp2 knockout mouse models, CSR assays in B cells, translocation frequency analysis |
The Journal of experimental medicine |
High |
19364882
|
| 2009 |
Parp2 interacts with transition protein TP2 and chaperone HSPA2 in spermatids; Parp2-TP2 interaction is partly mediated by poly(ADP-ribosyl)ation; Parp2 deficiency causes loss of TP2-expressing spermatids, defective chromatin condensation, abnormal manchette microtubules, and spermatid-specific cell death. |
In vitro protein-protein interaction assays, immunohistochemistry, electron microscopy, Parp2 KO mouse model |
Experimental cell research |
High |
19607827
|
| 2010 |
Crystal structure of the catalytic domain of human PARP2 in complex with PARP inhibitors (3-aminobenzamide and ABT-888) reveals structural features of the NAD+-binding catalytic pocket and provides basis for selective inhibitor design. |
X-ray crystallography |
Biochemistry |
High |
20092359
|
| 2011 |
PARP1 and PARP2 regulate topoisomerase II beta (TOP2B) activity during spermiogenesis; PARP1 and PARP2 activity strongly inhibits TOP2B in vitro, an effect counteracted by PAR glycohydrolase; pharmacological and genetic PARP inhibition increases TOP2B-DNA covalent binding in spermatids in vivo, suggesting a functional cycle regulating chromatin remodeling. |
In vitro TOP2B activity assay, in vivo TOP2B-DNA complex analysis by CsCl centrifugation, pharmacological and genetic inhibition of PARPs |
Biology of reproduction |
High |
21228215
|
| 2011 |
PARP-2 acts as a direct negative regulator of the SIRT1 promoter, independent of NAD+ levels; PARP-2 deficiency increases SIRT1 expression, promotes energy expenditure, increases mitochondrial content, and protects against diet-induced obesity, but causes glucose intolerance due to defective pancreatic function. |
PARP-2 KO mouse model, SIRT1 promoter reporter assays, metabolic phenotyping, NAD+ measurement |
Cell metabolism |
High |
21459329
|
| 2012 |
Clinical PARP inhibitors trap PARP1 and PARP2 at damaged DNA; trapped PARP-DNA complexes are more cytotoxic than unrepaired SSBs alone; trapping potency differs among inhibitors (niraparib > olaparib >> veliparib) in a pattern not correlated with catalytic inhibitory potency; repair of trapped PARP-DNA complexes requires homologous recombination, postreplication repair, Fanconi anemia pathway, polymerase β, and FEN1. |
PARP trapping assay (chromatin fractionation), cytotoxicity assays in DT40 cell lines with genetic deletions in specific repair genes |
Cancer research |
High |
23118055
|
| 2013 |
PARP-2 displays highest DNA-binding affinity for flap-containing DNA but is most efficiently activated by 5'-overhang DNA; PARP-2 inhibits DNA polymerase β activity but unlike PARP-1, its poly(ADP-ribosyl)ation does not restore DNA synthesis; PARP-2 inhibits FEN1 activity without PAR-dependent recovery; PARP-2 can also modulate PARP-1's poly(ADP-ribosyl)ation activity. |
EMSA, in vitro PARP activation assays with various DNA substrates, DNA polymerase β and FEN1 activity assays |
Biochimie |
High |
23357680
|
| 2013 |
PARP-2 is a suppressor of the SREBP1 promoter in a manner dependent on PARP-2 enzymatic activity; PARP-2 deletion increases SREBP1 and its target gene expression, leading to hepatic cholesterol accumulation and decreased HDL levels; ABCA1 expression is reduced in PARP-2-deficient cells/mice, linked to lower HDL. |
PARP-2 KO mouse model, PARP-2 siRNA knockdown in HepG2 cells, SREBP1 promoter reporter assay, lipid analysis |
Biochimica et biophysica acta |
High |
24365238
|
| 2014 |
PARP-2 and PARP-3 are preferentially activated by DNA breaks harboring a 5' phosphate group; the WGR domain is the central regulatory domain for DNA binding and activation of PARP-2 (and PARP-3), unlike PARP-1 where N-terminal zinc fingers are critical; PARP-1, PARP-2, and PARP-3 share an allosteric mechanism of DNA-dependent catalytic activation through local destabilization of the catalytic domain. |
Biochemical activity assays with defined DNA substrates, domain deletion and mutation analysis, biophysical binding assays |
Nucleic acids research |
High |
24928857
|
| 2014 |
PARP-2 deficiency in mice leads to chronic anemia due to replicative stress in erythroid progenitors, evidenced by micronuclei, γ-H2AX accumulation in S-phase, constitutive CHK1 and RPA phosphorylation; p53-dependent DNA damage response is activated; loss of pro-apoptotic PUMA restores hematocrit, while loss of p21 exacerbates fetal erythropoiesis failure. |
PARP-2 KO mouse model, γ-H2AX immunostaining, cell cycle analysis, double KO genetic epistasis (Parp2/Puma, Parp2/p21), transcriptome analysis |
Cell death and differentiation |
High |
25501596
|
| 2014 |
ARTD2 (PARP2) is activated by RNA in vitro; the N-terminal SAP domain is important for RNA binding; co-treatment with an RNA Pol I inhibitor substantially increases H2O2- or MNNG-induced PAR formation predominantly through ARTD2 and not ARTD1 in cells. |
In vitro PARP activity assay with RNA, ARTD1/ARTD2 siRNA knockdown in cells, PAR immunoblotting |
Nucleic acids research |
High |
24510188
|
| 2015 |
All three domains of PARP-2 (NTR, WGR, and CAT) collectively contribute to interaction with DNA damage; the NTR is natively disordered and only required for activation on specific DNA damage types; the WGR and CAT domains together are sufficient for PARP-2 recruitment to sites of DNA breaks in cells; NTR is not essential for cellular localization to damage sites. |
Biophysical binding assays, biochemical activity assays, X-ray crystallography (NTR structural characterization), live-cell imaging of domain deletion mutants at laser-induced damage sites |
Nucleic acids research |
High |
26704974
|
| 2015 |
PARP1 and PARP2 both bind DNA nicks at single-molecule level; PARP2 is mainly detected at single DNA nick sites with low affinity for undamaged DNA or DSBs; PARP2 dimer form is more effective in PAR synthesis; PARP2 suppresses PAR synthesis catalyzed by PARP1 after SSBs; activation of both PARPs leads to highly branched PAR synthesis whose size depends on SSBs (for PARP2) or SSBs/DSBs (for PARP1). |
Single-molecule AFM imaging, fluorescence titration, biochemical PAR synthesis assays |
Nucleic acids research |
High |
26673720
|
| 2017 |
PARP2 controls DSB repair pathway choice independently of PAR synthesis activity by limiting 53BP1 accumulation at DNA damage sites, thereby promoting CtIP-dependent DNA end-resection and channeling repair toward HR, SSA, and alternative end-joining rather than canonical NHEJ. |
PARP2 KO and catalytic mutant cell lines, 53BP1 foci analysis, CtIP-dependent resection assay, reporter assays for different repair pathways |
Nucleic acids research |
High |
29036662
|
| 2017 |
Either PARP1 or PARP2 is sufficient for near-normal XRCC1 recruitment to oxidative SSBs; loss of both PARP1 and PARP2 is required to greatly reduce or ablate XRCC1 and PNKP chromatin binding after H2O2 treatment; very low levels of ADP-ribosylation produced by either enzyme are sufficient for XRCC1 recruitment. |
PARP1/PARP2 isogenic deletion cell lines, XRCC1 and PNKP chromatin fractionation after H2O2, PARP inhibitor dose-response |
Nucleic acids research |
High |
27965414
|
| 2018 |
PARP2 is preferentially activated by PAR chains and subsequently catalyzes branched PAR chain synthesis; the N-terminus of PARP2 directly binds PAR to promote branched PAR synthesis; the PBZ domain of APLF recognizes branched PAR chains and regulates chromatin remodeling at DNA damage sites. |
In vitro PAR binding and activity assays, PAR chain structure analysis, APLF PBZ domain binding assay, chromatin remodeling assays |
Nature communications |
High |
30104678
|
| 2018 |
PARP2 (and PARP3) can poly(ADP-ribosyl)ate 5'- and 3'-terminal phosphate residues at double- and single-strand break termini of DNA molecules (DNA ADP-ribosylation); PARP-mediated DNA ADP-ribosylation can be more effective than auto-ADP-ribosylation depending on DNA substrates; persisting anti-PAR signals are detected in genomic DNA from bleomycin-treated PARG-depleted cells. |
In vitro ADP-ribosylation assays with defined DNA substrates, anti-PAR antibody detection in purified genomic DNA, cell-free extract assays |
Nucleic acids research |
High |
29361132
|
| 2018 |
PARP2 is required to stabilize replication forks that encounter BER intermediates; PARP2 acts through Fbh1-dependent regulation of Rad51 to stabilize Rad51 at damaged replication forks and prevent uncontrolled DNA resection; combined PARP1 and PARP2 disruption leads to defective BER and elevated replication-associated DNA damage. |
PARP1 and PARP2 knockout cell lines, replication fork stability assays (DNA fiber), Rad51 foci analysis, genetic epistasis with Fbh1 |
Nature communications |
High |
29467415
|
| 2018 |
Crystal structures of ARTD2 (PARP2) WGR domain bound to DSB-mimicking DNA oligonucleotides reveal that the WGR domain mediates DNA end-to-end interaction, recognizes the 5'-phosphate group, and can mediate joining of DNA ends; extensive mutagenesis confirmed that the WGR domain is the key DNA break detection module. |
X-ray crystallography, site-directed mutagenesis, activity assays, binding assays, stoichiometry measurements |
Nucleic acids research |
High |
30321391
|
| 2019 |
PARP-2 (but not PARP-1) is a critical component of the androgen receptor (AR) transcriptional machinery through interaction with the pioneer factor FOXA1; PARP-2 facilitates AR recruitment to prostate-specific enhancer regions genome-wide; selective targeting of PARP-2 blocks PARP-2/FOXA1 interaction, attenuates AR-mediated gene expression, and inhibits AR-positive prostate cancer growth. |
Co-immunoprecipitation, ChIP-seq for AR and PARP-2, PARP-2 knockout/knockdown, prostate cancer growth assays |
Proceedings of the National Academy of Sciences of the United States of America |
High |
31266892
|
| 2020 |
Cryo-EM structure of human PARP2-HPF1 bound to a nucleosome shows that PARP2-HPF1 bridges two nucleosomes with broken DNA aligned for ligation; bridging induces structural changes in PARP2 signaling DNA break recognition to the catalytic domain, which licenses HPF1 binding and PARP2 activation; HPF1 switches PARP2 amino acid specificity from aspartate/glutamate to serine; active PARP2 cycles through conformational states to exchange NAD+ and substrate. |
Cryo-electron microscopy structure determination, biochemical activation assays |
Nature |
High |
32939087
|
| 2020 |
Cryo-EM structure of PARP2 bridging two nucleosomes via short linker DNA at DSBs; PARP2 bridges DNA ends in the nucleosome context; this conformation provides a binding platform for HPF1; the resulting HPF1·PARP2·nucleosome complex is enzymatically active. |
Cryo-EM structure determination, enzymatic activity assays of the complex |
PloS one |
High |
33141820
|
| 2020 |
The ALC1 (CHD1L) helicase is strictly required for PARP2 release from DNA lesions; catalytic inactivation of ALC1 quantitatively traps PARP2 (but not PARP1) at DNA breaks; ALC1 manipulation potentiates PARPi-induced cancer cell killing and mediates synthetic lethality upon BRCA deficiency through PARP2 trapping. |
Live-cell imaging of PARP2 foci, ALC1 catalytic mutant, PARP inhibitor treatment, BRCA-deficient cell lines |
Molecular cell |
High |
33275888
|
| 2021 |
Crystal structure of PARP2 in complex with 5'-phosphorylated activating DNA shows that the WGR domain bridges the dsDNA gap and joins DNA ends; DNA binding induces conformational changes including reorganization of helical fragments in the regulatory domain relieving autoinhibition; the active conformation enables NAD+ binding and HPF1 binding that shifts residue specificity from glutamate to serine. |
X-ray crystallography, NAD+ binding assay, HPF1 binding assay |
Nature communications |
High |
34108479
|
| 2021 |
HPF1 has a dual function: it stimulates PARP2 autoPARylation and heteroPARylation of histones in the nucleosome complex at defined HPF1/NAD+ concentrations, while at other concentrations it limits PARylation; PARP2 is more efficiently stimulated by HPF1 than PARP1 in autoPARylation and is more active in histone heteroPARylation than automodification. |
In vitro PARylation assays with purified components, nucleosome reconstitution, concentration-response analysis |
Communications biology |
High |
34732825
|
| 2021 |
Combined PARP-1 and PARP-2 deficiency in the uterus leads to pregnancy loss through decidualization failure; absence of both enzymes increases p53 signaling and senescent decidual cell population; embryo attachment and luminal epithelium removal are normal, but subsequent decidualization fails. |
Uterine-specific Parp1/Parp2 double KO mice, histological and molecular analysis of decidualization |
Proceedings of the National Academy of Sciences of the United States of America |
High |
34580230
|
| 2021 |
PARP2 predominantly functions in single-strand break repair at actively transcribed DNA regions; CSB promotes recruitment of XRCC1 and HPF1 and histone PARylation; CSB's function in SSBR is largely bypassed when transcription is inhibited; CSB regulates SSBR mediated by both PARP1 and PARP2 but PARP2's function is specifically coupled to transcriptionally active regions. |
Chromatin co-fractionation, alkaline comet assay, transcription inhibition experiments, PARP1/PARP2 knockdown/KO |
Nucleic acids research |
High |
37326017
|
| 2022 |
PARP inhibitors trap PARP2 by switching its recruitment mode from a predominantly PARP1- and PAR-dependent rapid exchange to a WGR domain-mediated stalling on DNA; PARP2-R140A (WGR mutant) and H415A (catalytic mutant) abolish PARP inhibitor-induced PARP2 trapping; in PARP1-deficient cells, PARP2 forms DNA-dependent, PAR-independent foci. |
Live-cell imaging, PARP1 deletion cells, WGR and catalytic domain point mutants, PARP inhibitor treatment (niraparib, talazoparib, olaparib) |
Nucleic acids research |
High |
35349716
|
| 2023 |
Clinical PARP inhibitors exert an allosteric effect that retains PARP2 on DNA breaks; this allosteric retention depends on communication between the catalytic and DNA-binding regions of PARP2; a PARP2 mutant mimicking the allosteric inhibitor effect shows increased cellular retention at damage sites; AZD5305 exhibits a reverse allosteric effect on PARP2. |
PARP2 mutant biochemical assays, live-cell imaging at damage sites, structure-activity analysis of clinical PARPis |
Science advances |
High |
36961901
|
| 2023 |
PARP2 forms a mechanically stable bridge (~85 pN rupture force) across blunt-end 5'-phosphorylated DSBs, restoring torsional continuity; PARP2 switches between bridging and end-binding modes depending on DNA end structure (blunt vs. overhang); PARP1 does not bridge DSBs and competes away PARP2 bridge formation. |
Single-molecule magnetic tweezers force spectroscopy |
Proceedings of the National Academy of Sciences of the United States of America |
High |
37216533
|
| 2024 |
PARP2 is selectively recruited and activated by 5'-phosphorylated nicks (5'p-nicks), including those between Okazaki fragments; DNA replication robustly activates PARP2 (more than DNA damage); catalytically inactive PARP2 (E534A) but not its absence impedes Lig1- and Lig3-mediated nick ligation, causing dose-dependent replication fork collapse specifically in erythroblasts; this PARylation-dependent structural function at 5'p-nicks explains PARPi-induced anemia. |
Parp2 catalytic mutant knock-in mouse (Parp2EA/EA), genetic epistasis with Lig1 KO, replication fork analysis, erythropoiesis phenotyping, Tp53/Chk2 double KO epistasis |
Molecular cell |
High |
39383878
|
| 2024 |
PARP2 promotes replication stress-induced telomere fragility via the break-induced replication (BIR) pathway; PARP2 promotes DNA end resection, strand invasion, and BIR-dependent mitotic DNA synthesis by orchestrating POLD3 recruitment and activity at telomeres. |
PARP2 depletion, BIR reporter assay, POLD3 recruitment analysis, telomere fragility assay, oxidative lesion induction |
Nature communications |
High |
38565848
|
| 2013 |
PARP-2 regulates cell cycle-related gene expression through transcriptional repression independently of its enzymatic PARylation activity; PARP-2 interacts with and recruits histone deacetylases HDAC5 and HDAC7 and histone methyltransferase G9a to promoters, generating repressive chromatin signatures. |
Co-immunoprecipitation, ChIP assays, PARP-2 catalytic mutant, gene expression analysis |
Biochemical and biophysical research communications |
Medium |
23291187
|
| 2016 |
ARTD2 (PARP2) binds damaged DNA as both monomer and dimer; the N-terminus functions as a high-affinity DNA-binding module while the WGR domain contributes to DNA binding specificity and catalytic activation; ARTD2 is preferentially activated by short 5'-phosphorylated DNA oligonucleotides; in DSB repair ARTD2 likely functions as a dimeric module and in SSB repair as a monomer. |
Solution structure studies (SAXS), biophysical binding measurements (SPR, fluorescence), biochemical activity assays |
Scientific reports |
High |
27708353
|
| 2019 |
PARP2 binds the early BER intermediates at single-molecule level; both PARP1 and PARP2 efficiently interact with DNA nicks; PARP2 suppresses PAR synthesis by PARP1 after SSBs; PARP2 dimer form is more effective at PAR synthesis. |
Single-molecule AFM imaging of BER intermediate DNA substrates |
Journal of molecular biology |
High |
31129062
|
| 2020 |
Myeloid deletion of PARP2 (but not PARP1) increases immature myeloid cells in bone marrow and impairs CCL3 chemokine expression by enhancing transcriptional repression by β-catenin; compromised CCL3 production creates an immune-suppressive milieu, increasing breast cancer bone metastasis; olaparib treatment increases bone metastasis through PARP2 in the myeloid lineage. |
Myeloid-specific PARP2 conditional KO mice, β-catenin ChIP, CCL3 expression analysis, breast cancer bone metastasis model |
Nature communications |
High |
32221289
|
| 2020 |
Silencing of PARP2 blocks autophagic degradation in C2C12 myoblasts; PARP2 deficiency inhibits AMPK and mTORC2 activity; rescue with AICAR (AMPK activator), NAD+ precursor, or SIRT1 inhibitor decreases the number of LC3-positive vesicles, linking PARP2 to autophagic flux via AMPK/SIRT1 pathway; PARP2 enzymatic activity is important for regulating autophagy. |
PARP2 shRNA in C2C12 cells, primary PARP2 KO MEFs, LC3 immunostaining, electron microscopy, AMPK/mTORC2 activity assays, pharmacological rescue |
Cells |
Medium |
32046043
|
| 2021 |
PARP2 forms more dynamic complexes with BER protein partners (PARP1, APE1, Polβ, XRCC1) compared to PARP1; the major form of PARP2 at excess PARP1 is their heterocomplex; PARP2 activity is more strongly inhibited by XRCC1 than PARP1; the activity of both PARP1 and PARP2 is suppressed upon heteroPARylation; PARP2 can function via an alternative XRCC1-independent mechanism through hetero-oligomerization with PARP1. |
Fluorescence-based binding assays, light scattering for oligomeric state, in vitro PAR synthesis assays with BER protein partners |
International journal of molecular sciences |
High |
33925170
|
| 2015 |
PARP-2 interacts with AP (abasic) sites via Schiff base formation through its N-terminal domain; PARP-2 binding to AP sites inhibits APE1 activity; unlike PARP-1, PARP-2's inhibitory influence on APE1 is not modulated by PAR synthesis; PARP-2 has 5'-dRP lyase activity comparable to PARP-1 but much weaker than Pol β. |
AP site cross-linking assay, APE1 activity assay, dRP lyase assay |
Biochimie |
High |
25724268
|