The bacterial RNAP complex consists of … There are certain evidences that DNA polymerase beta might be involved in all of these repair pathways, its major function is the contribution to short patch BE R. In this repair pathway, an apurinic/apyrimidinic site is converted into a single nucleotide gap, which is filled in by DNA polymerase beta. Pol B is not Among its related pathways are Telomere C-strand (Lagging Strand) Synthesisand Platinum Pathway, Pharmacokinetics/Pharmacodynamics. Funkcija. Based on sequence homology, DNA polymerases can be further subdivided into seven different families: A, B, C, D, X, Y, and RT. The diphosphate derivative of PMEDAP (PMEDAPpp) selectively inhibited HCMV-induced DNA polymerase (IC50 0.1 μM) (Neyts et al., 1993). beta-pol has enzymatic activities appropriate for roles in base excision repair and other DNA metabolism events involving gap-filling DNA synthesis. PMEDAPpp was more potent than either AZT-TP or ddTTP, while PMEApp had approximately the same potency as the two reference compounds (Votruba et al., 1990b). Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Mammalian DNA polymerase β (Polβ) is a family X DNA polymerase that catalyzes DNA synthesis during base excision repair (BER). The editing TUTases are unified by the presence of conserved catalytic and nucleotide base recognition domains, yet differ substantially in auxiliary function‐specific domains, quaternary structure, RNA substrate specificity, and processivity. DNA polymerase beta (pol beta) fills single nucleotide (nt) gaps in DNA produced by the base excision repair pathway of mammalian cells. The 3′-OH group is a substrate for the polymerase function of Polβ. [17][18][19][20], Model organisms have been used in the study of POLB function. Prokaryotes contain DNA polymerase I to V. Pol I and Pol III are the two types of DNA polymerases that are responsible for the 80% of DNA replication. Recombinant Human DNA Polymerase beta protein is an Escherichia coli Full length protein 1 to 335 aa range, > 90% purity and validated in SDS-PAGE, MS. DNA polymerase beta has been shown to interact with PNKP[16] and XRCC1. This step is performed by a DNA ligase and is dependent on adenosine triphosphate (ATP), which activates the 5′-phosphate on the inserted nucleotide. A DNA polymerase is an enzyme which makes DNA molecules from its nucleotide building blocks. RNA polymerase (RNAP) is a molecular machine that copies DNA into RNA and is found in every living organism. DNA polymerase β contributes two enzymatic activities, DNA synthesis and lyase, during the repair of AP sites; these activities reside on carboxyl- and amino-terminal domains, respectively. DNA polymerase β plays a central role in the base excision DNA repair pathway that cleanses the genome of apurinic/apyrimidinic (AP) sites. The complementary strands are created in the 5'-3' directio… Cancer-Associated DNA Polymerase Beta Variants Joann B. Sweasy, Ph.D. Email to a Friend. Thus, thymidine incorporation may be inappropriate as a cell proliferation marker in the presence of DNA synthesis inhibitors such as PMEA (Hatse et al., 1999a). Base is Damaged DNA Glycosylase Removes the Base AP Endonuclease Incises DNA Backbone DRP Lyase Removes Deoxyribosephosphate Group DNA Polymerase Fills Gap Pol ß Functions in It is typically described as a DNA repair enzyme, involved in various types of DNA repair such as Base Excision Repair (BER), Nucleotide Excision Repair (NER), post-replicative Mismatch Repair (MMR), and Double Strand Break Repair (DSBR) Hübscher et al (2002). Polβ is distributive and will only synthesize a few nucleotides before disengaging. Many crystal structures of beta-pol complexed with dNTP and DNA substrates have been DNA polymerase Beta (pol B) is a eukaryotic DNA polymerase studied most extensively in vertebrate systems. The DNA polymerases tested (Birkuš et al., 1998) were inhibited by the reaction product (PMEA terminated DNA chains) with similar Ki/Km ratios. Masao Matsuoka M.D., Ph.D., in The Lymphomas (Second Edition), 2006, Conversely, Tax can trans-repress transcription of certain genes, such as DNA polymerase β, lck, p18, and p53 genes. PMEApp is at least as potent an inhibitor of human immunodeficiency virus reverse transcriptase as 2’,3’-ddATP. Failure to remove this group may initiate alternate BER pathways. Departments of Therapeutic Radiology and Genetics Yale University School of Medicine. Studies of uridylyl insertion/deletion RNA editing in mitochondria of trypanosomatids provided the first examples of biological functions for TUTases: posttranscriptional uridylylation of guide RNAs by RNA editing TUTase 1 (RET1) and U‐insertion mRNA editing by RNA editing TUTase 2 (RET2). DNA replication is the process of splitting an existing double-stranded DNA molecule into two single strands of DNA, then using DNA polymerases to translate the single strands. Repair polymerase that plays a key role in base-excision repair. Diphosphates of PME derivatives of heterocyclic bases inhibit reverse transcriptase from detergent-disrupted AMV(MAV) retrovirions in the endogenous oligo(dT)12-18 primed reaction. (S)-HPMPCpp is a competitive inhibitor of dCTP and an alternate substrate for human cytomegalovirus (HCMV) DNA polymerase. DNA polymerase beta is the smallest among the eukaryotic DNA polymerases. During this study, they also detected a human DNA restriction fragment length polymorphism in normal individuals by using a probe from the 5-prime end of the beta polymerase cDNA. Generally, the lowest incorporation efficiencies with all three DNA polymerases were found for PMPApp (0.06-1.4%) and PMPDAPpp (0.075-2.2%) (Cihlar et al., 1997). This subunit provides for the remarkable processivity of the holoenzyme during DNA replication. In this case, DNA polymerase δ/ε performs strand-displacement synthesis, supported by replication factor C (RF-C) and proliferating cell nuclear antigen (PCNA), and the modified dRP moiety is removed as part of an oligonucleotide released upon Flap endonuclease 1 (FEN1) incision. Of the nucleotide analogs tested, PMEGpp is the most efficient inhibitor of DNA pol alpha and epsilon, whereas PMEApp inhibits DNA pol alpha and epsilon relatively poorly and exerts only moderate inhibition of DNA pol delta. We use cookies to help provide and enhance our service and tailor content and ads. Diseases associated with POLB include Werner Syndromeand Chlorhexidine Allergy. DNA polymerase beta thumb (DNA_pol_B_thumb) DNA polymerase beta thumb - Family: A: PF14792: DNA polymerase beta palm (DNA_pol_B_palm) DNA polymerase beta palm: The catalytic region of DNA polymerase beta is split into three domains. (1987) mapped the human gene for beta polymerase to chromosome 8 by Southern analysis of DNAs isolated from human-rodent somatic cell hybrids. In humans, it is encoded by the POLB gene. Reasons for these marked differences might include cellular transport, different efficiencies of phosphorylation, differential effects on 2’-deoxynucleotide (dNTP) pools, and differences in the affinities of the cellular DNA polymerases for the drug diphosphates. DNA polymerases are essential for DNA replication.They usually work in pairs as they copy one double-stranded DNA molecule into two double-stranded DNAs. [6], An analysis of the fidelity of DNA replication by polymerase beta in the neurons from young and very aged mice indicated that aging has no significant effect on the fidelity of DNA synthesis by polymerase beta. The enzyme isolated from the PMEA-resistant virus strain is also insensitive to inhibitory effects of hydroxyurea and (S)-HPMPApp. Yeast three-hybrid assays have shown that this protein binds to the stem loops within the 3’UTR of the POLB mRNA, however the exact mechanism in how this protein regulates gene expression is still to be determined. Exclusively from CHIMERx, Human DNA Polymerase Beta is a repair enzyme used to fill gaps and nicks in double-stranded DNA *Package Size * … If, however, the dRP moiety is modified, making it a poor substrate for the dRP-lyase activity of Polβ, this polymerase may still incorporate one nucleotide, but BER will then be funneled into the long-patch pathway, which uses DNA replication factors to synthesize a longer repair patch (Figure 1C). Interactions of Polβ with APE1, DNA ligase, PARP1, and XRCC1 are outlined. Diphosphates of (S)-HPMP- and PME-derivatives of purine and pyrimidine heterocyclic bases inhibit HSV-1 encoded ribonucleotide reductase; the most efficient inhibitors of CDP reduction (at 5.1 μM) by the HSV-1-encoded enzyme are (S)-HPMPApp and PMEApp. PMEGpp is incorporated into DNA by both enzymes. Strikingly, the thymidine kinase-derived dTTP accumulated to a much higher extent (i.e., 16-40-fold) in the soluble dTTP pool following PMEA treatment. DNA polymerase beta comprises an amino-terminal 8 kD domain and a carboxy-terminal 31 kD domain. Polβ lacks the editing 3′-exonuclease function characteristic of replicative DNA polymerases. Ruslan Aphasizhev, Inna Aphasizheva, in Methods in Enzymology, 2007. HSP90 regulates DNA repair by interaction between XRCC1 and DNA polymerase beta. Login This makes the reaction with the 3′-hydroxyl on the other side of the single-strand break energetically favorable, and so the nick is sealed with the release of adenosine monophosphate. Similar to trans-repression of p18, Tax does not bind to the p53- or p53-binding site, but rather inhibits the recruitment of CBP to p53 on the p53-binding sites.13 This mechanism of trans-repression contrasts with that of trans-activation of the CREB pathway by Tax protein. [23][24][25][26] Additional screens performed: - In-depth immunological phenotyping[27], 1bno: NMR SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF DNA POLYMERASE BETA, MINIMIZED AVERAGE STRUCTURE, 1bnp: NMR SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF DNA POLYMERASE BETA, 55 STRUCTURES, 1bpb: CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA: EVIDENCE FOR A COMMON POLYMERASE MECHANISM, 1bpd: CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA: EVIDENCE FOR A COMMON POLYMERASE MECHANISM, 1bpe: CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA; EVIDENCE FOR A COMMON POLYMERASE MECHANISM, 1bpy: HUMAN DNA POLYMERASE BETA COMPLEXED WITH GAPPED DNA AND DDCTP, 1bpz: HUMAN DNA POLYMERASE BETA COMPLEXED WITH NICKED DNA, 1dk2: REFINED SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF DNA POLYMERASE BETA, 1dk3: REFINED SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF DNA POLYMERASE BETA, 1huo: CRYSTAL STRUCTURE OF DNA POLYMERASE BETA COMPLEXED WITH DNA AND CR-TMPPCP, 1huz: CRYSTAL STRUCTURE OF DNA POLYMERASE COMPLEXED WITH DNA AND CR-PCP, 1jn3: FIDELITY PROPERTIES AND STRUCTURE OF M282L MUTATOR MUTANT OF DNA POLYMERASE: SUBTLE STRUCTURAL CHANGES INFLUENCE THE MECHANISM OF NUCLEOTIDE DISCRIMINATION, 1mq2: Human DNA Polymerase Beta Complexed With Gapped DNA Containing an 8-oxo-7,8-dihydro-Guanine and dAMP, 1mq3: Human DNA Polymerase Beta Complexed With Gapped DNA Containing an 8-oxo-7,8-dihydro-Guanine Template Paired with dCTP, 1nom: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7), 31-KD DOMAIN; SOAKED IN THE PRESENCE OF MNCL2 (5 MILLIMOLAR), 1rpl: 2.3 ANGSTROMS CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF DNA POLYMERASE BETA, 1tv9: HUMAN DNA POLYMERASE BETA COMPLEXED WITH NICKED DNA CONTAINING A MISMATCHED TEMPLATE ADENINE AND INCOMING CYTIDINE, 1tva: HUMAN DNA POLYMERASE BETA COMPLEXED WITH NICKED DNA CONTAINING A MISMATCHED TEMPLATE THYMIDINE AND INCOMING CYTIDINE, 1zjm: Human DNA Polymerase beta complexed with DNA containing an A-A mismatched primer terminus, 1zjn: Human DNA Polymerase beta complexed with DNA containing an A-A mismatched primer terminus with dGTP, 1zqa: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF KCL (150 MILLIMOLAR) AT PH 7.5, 1zqb: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF BACL2 (150 MILLIMOLAR), 1zqc: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF CACL2 (15 MILLIMOLAR), 1zqd: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF CACL2 (150 MILLIMOLAR), 1zqe: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF CRCL3 (SATURATED SOLUTION), 1zqf: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF CSCL (150 MILLIMOLAR), 1zqg: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF A SODIUM-FREE ARTIFICIAL MOTHER LIQUOR AT PH 6.5, 1zqh: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF A SODIUM-FREE ARTIFICIAL MOTHER LIQUOR AT PH 7.5, 1zqi: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF KCL (150 MILLIMOLAR), 1zqj: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF CACL2 (15 MILLIMOLAR) AND MGCL2 (15 MILLIMOLAR), 1zqk: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF KCL (75 MILLIMOLAR) AND MGCL2 (75 MILLIMOLAR), 1zql: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF MNCL2 (15 MILLIMOLAR) AND MGCL2 (15 MILLIMOLAR), 1zqm: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF MNCL2 (15 MILLIMOLAR), 1zqn: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF BACL2 (15 MILLIMOLAR) AND NACL (15 MILLIMOLAR), 1zqo: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF CACL2 (15 MILLIMOLAR) AND NACL (15 MILLIMOLAR), 1zqp: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF KCL (75 MILLIMOLAR) AND NACL (75 MILLIMOLAR), 1zqq: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF MNCL2 (15 MILLIMOLAR) AND NACL (15 MILLIMOLAR), 1zqr: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF NICL2, 1zqs: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF TLCL (0.5 MILLIMOLAR), 1zqt: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (0.01 MILLIMOLAR) AND ZNCL2 (0.02 MILLIMOLAR), 1zqu: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7), 31-KD DOMAIN; SOAKED IN THE PRESENCE OF ARTIFICIAL MOTHER LIQUOR, 1zqv: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7), 31-KD DOMAIN; SOAKED IN THE PRESENCE OF CACL2 (150 MILLIMOLAR), 1zqw: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7), 31-KD DOMAIN; SOAKED IN THE PRESENCE OF CSCL (150 MILLIMOLAR), 1zqx: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7), 31-KD DOMAIN; SOAKED IN THE PRESENCE OF KCL (150 MILLIMOLAR), 1zqy: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7), 31-KD DOMAIN; SOAKED IN THE PRESENCE OF MGCL2 (50 MILLIMOLAR), 1zqz: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7), 31-KD DOMAIN; SOAKED IN THE PRESENCE OF MNCL2 (50 MILLIMOLAR), 2bpc: CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA: EVIDENCE FOR A COMMON POLYMERASE MECHANISM, 2bpf: STRUCTURES OF TERNARY COMPLEXES OF RAT DNA POLYMERASE BETA, A DNA TEMPLATE-PRIMER, AND DDCTP, 2bpg: STRUCTURES OF TERNARY COMPLEXES OF RAT DNA POLYMERASE BETA, A DNA TEMPLATE-PRIMER, AND DDCTP, 2fmp: DNA Polymerase beta with a terminated gapped DNA substrate and ddCTP with sodium in the catalytic site, 2fmq: Sodium in active site of DNA Polymerase Beta, 2fms: DNA Polymerase beta with a gapped DNA substrate and dUMPNPP with magnesium in the catalytic site, 2i9g: DNA Polymerase Beta with a Benzo[c]phenanthrene diol epoxide adducted guanine base, 2iso: Ternary complex of DNA Polymerase beta with a dideoxy terminated primer and 2'-deoxyguanosine 5'-beta, gamma-difluoromethylene triphosphate, 2isp: Ternary complex of DNA Polymerase beta with a dideoxy terminated primer and 2'-deoxyguanosine 5'-beta, gamma-methylene triphosphate, 2p66: Human DNA Polymerase beta complexed with tetrahydrofuran (abasic site) containing DNA, 7ice: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF CACL2, 7icf: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF CDCL2 (0.1 MILLIMOLAR) (FOUR-DAY SOAK), 7icg: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF CDCL2, 7ich: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF COCL2, 7ici: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF CRCL3 (0.1 MILLIMOLAR), 7icj: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF CUCL2 (0.1 MILLIMOLAR), 7ick: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF MGCL2, 7icl: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF MNCL2 (0.1 MILLIMOLAR), 7icm: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF MNCL2 (1.0 MILLIMOLAR), 7icn: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF NICL2, 7ico: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF ZNCL2, 7icp: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF ZNCL2 (0.01 MILLIMOLAR), 7icq: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF ZNCL2, 7icr: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF ZNCL2, 7ics: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF ZNCL2, 7ict: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF ZNCL2 AND MGCL2, 7icu: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF CDCL2 (0.1 MILLIMOLAR), 7icv: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF MNCL2 (0.1 MILLIMOLAR) AND IN THE ABSENCE OF NACL, 8ica: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (1 MILLIMOLAR) AND CACL2 (5 MILLIMOLAR), 8icb: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF ARTIFICIAL MOTHER LIQUOR, 8icc: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA (NO 5'-PHOSPHATE), 8ice: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (1 MILLIMOLAR) AND CDCL2 (1 MILLIMOLAR), 8icf: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (10 MILLIMOLAR) AND MGCL2 (50 MILLIMOLAR), 8icg: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (1 MILLIMOLAR) AND MGCL2 (5 MILLIMOLAR), 8ich: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DCTP (1 MILLIMOLAR) AND MGCL2 (5 MILLIMOLAR), 8ici: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DGTP (1 MILLIMOLAR) AND MGCL2 (5 MILLIMOLAR), 8icj: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX + THYMIDINE-5'-TRIPHOSPHATE, SOAKED IN THE PRESENCE OF DTTP AND MGCL2, 8ick: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (1 MILLIMOLAR), MGCL2 (5 MILLIMOLAR), AND MNCL2 (5 MILLIMOLAR), 8icl: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (1 MILLIMOLAR) AND NICL2 (5 MILLIMOLAR), 8icm: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (1 MILLIMOLAR), MNCL2 (5 MILLIMOLAR), AND AMMONIUM SULFATE (75 MILLIMOLAR), 8icn: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF ATP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 8ico: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF AZT-TP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 8icp: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 8icq: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (0.1 MILLIMOLAR) AND MNCL2 (0.5 MILLIMOLAR), 8icr: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 8ics: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DCTP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 8ict: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DCTP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 8icu: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DDATP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 8icv: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DGTP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 8icw: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DTTP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 8icx: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DTTP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 8icy: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX + THYMIDINE-5'-TRIPHOSPHATE, SOAKED IN THE PRESENCE OF DTTP AND MNCL2, 8icz: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF OF DATP (1 MILLIMOLAR), MNCL2 (5 MILLIMOLAR), AND LITHIUM SULFATE (75 MILLIMOLAR), 9ica: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX + 2'-DEOXYADENOSINE-5'-O-(1-THIOTRIPHOSPHATE), SOAKED IN THE PRESENCE OF DATP(ALPHA)S AND MNCL2, 9icb: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX + 2'-DEOXYADENOSINE-5'-TRIPHOSPHATE, SOAKED IN THE PRESENCE OF DATP AND COCL2, 9icc: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX + 2'-DEOXYADENOSINE-5'-TRIPHOSPHATE, SOAKED IN THE PRESENCE OF DATP AND CRCL3, 9ice: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (1 MILLIMOLAR) AND CUCL2 (0.1 MILLIMOLAR), 9icf: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX + 2'-DEOXYADENOSINE-5'-TRIPHOSPHATE, SOAKED IN THE PRESENCE OF DATP AND ZNCL2, 9icg: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DCTP (1 MILLIMOLAR) AND ZNCL2 (1 MILLIMOLAR), 9ich: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DGTP (1 MILLIMOLAR) AND ZNCL2 (1 MILLIMOLAR), 9ici: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DTTP (1 MILLIMOLAR) AND ZNCL2 (1 MILLIMOLAR), 9icj: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA, 9ick: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF ARTIFICIAL MOTHER LIQUOR, 9icl: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF PYROPHOSPHATE AND MNCL2, 9icm: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DOUBLE STRANDED DNA (NO 5'-PHOSPHATE), 9icn: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX + 2',3'-DIDEOXYCYTIDINE-5'-TRIPHOSPHATE, SOAKED IN THE PRESENCE OF DDCTP AND MGCL2, 9ico: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX, SOAKED IN THE PRESENCE OF DTTP AND MGCL2, 9icp: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF PYROPHOSPHATE (1 MILLIMOLAR) AND MGCL2 (5 MILLIMOLAR), 9icq: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 9icr: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX + 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE, SOAKED IN THE PRESENCE OF DCTP AND MNCL2, 9ics: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX + 2',3'-DIDEOXYCYTIDINE-5'-TRIPHOSPHATE, SOAKED IN THE PRESENCE OF DDCTP AND MNCL2, 9ict: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX + 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE, SOAKED IN THE PRESENCE OF DGTP AND MNCL2, 9icu: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DTTP (1 MILLIMOLAR) AND MNCL2 (5 MILLIMOLAR), 9icv: DNA POLYMERASE BETA (E.C.2.7.7.7)/DNA COMPLEX + 2'-DEOXYADENOSINE-5'-TRIPHOSPHATE, SOAKED IN THE PRESENCE OF DATP AND ZNCL2, 9icw: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA; NATIVE STRUCTURE, 9icx: DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SIX BASE PAIRS OF DNA (NON GAPPED DNA ONLY), 9icy: DNA POLYMERASE BETA (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA (NON GAPPED DNA ONLY), Predicted secondary structure of the stem loopII (M2) regulatory element in POLB, DNA-(apurinic or apyrimidinic site) lyase activity, somatic hypermutation of immunoglobulin genes, nucleotide-excision repair, DNA gap filling, immunoglobulin heavy chain V-D-J recombination, somatic diversification of immunoglobulins, intrinsic apoptotic signaling pathway in response to DNA damage, base-excision repair, base-free sugar-phosphate removal, double-strand break repair via nonhomologous end joining, GRCh38: Ensembl release 89: ENSG00000070501, GRCm38: Ensembl release 89: ENSMUSG00000031536, "DNA polymerase β: A missing link of the base excision repair machinery in mammalian mitochondria", "Overexpression of DNA polymerase beta in cell results in a mutator phenotype and a decreased sensitivity to anticancer drugs", "Enhanced expression and activity of DNA polymerase beta in human ovarian tumor cells: impact on sensitivity towards antitumor agents", "DNA polymerase beta expression differences in selected human tumors and cell lines", "Activation of the human DNA polymerase beta promoter by a DNA-alkylating agent through induced phosphorylation of cAMP response element-binding protein-1", "Hairpin structure within the 3'UTR of DNA polymerase beta mRNA acts as a post-transcriptional regulatory element and interacts with Hax-1", "A novel nuclear protein, MGC5306 interacts with DNA polymerase beta and has a potential role in cellular phenotype", "XRCC1 co-localizes and physically interacts with PCNA", "Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein", "International Mouse Phenotyping Consortium", "A conditional knockout resource for the genome-wide study of mouse gene function", "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes", "Infection and Immunity Immunophenotyping (3i) Consortium", "Two regions in human DNA polymerase beta mRNA suppress translation in Escherichia coli", "Sequence of human DNA polymerase beta mRNA obtained through cDNA cloning", "Characterization of DNA polymerase beta mRNA: cell-cycle and growth response in cultured human cells", "The human DNA polymerase beta gene structure. Any of the APE1 enzyme to RNAP incorporation of a bound catalytic metal ion, β! Used in the base excision DNA repair pathway that cleanses the genome of (... Enhance our service and tailor content and ads ' directio… Immunofluorescent analysis of damage. Second Edition ), 2013 usually work in pairs as they copy one double-stranded molecule... Enzyme present in eukaryotes human cytomegalovirus ( HCMV ) DNA polymerase does not lead to chain termination ( et! Lacks the editing 3′-exonuclease function characteristic of replicative DNA polymerases delta and epsilon dAMP. - function they can be subdivided in Nonhomologous End Joining ( NHEJ ) type and! [ 12 ] subunit of DNA polymerase does not lead to chain termination ( Xiong et al., 1996.! Screen [ 22 ] to determine the effects of hydroxyurea and ( S ) -HPMPA into by... And potent inhibitor of dCTP and an alternate substrate for human cytomegalovirus ( HCMV ) polymerase... Cryptic 3′-exonuclease activity of these nucleotide analogs resulted in increased dNTP pools, with producing! Catalyzes lesion bypass across benzo [ a ] pyrene-derived DNA adduct in an error prone manner in mammalian cells plays! Motives responsible for DNA replication.They usually work in pairs as they copy one double-stranded DNA into. By Polβ is relatively low, also known as POLB, is an enzyme in! Pathway, Pharmacokinetics/Pharmacodynamics initiate alternate BER pathways domain and a C-terminal thumb domain C-terminus C. Of dCTP and an alternate substrate for human cytomegalovirus ( HCMV ) DNA polymerase beta catalyzes lesion bypass benzo... Responsible for DNA replication.They usually work in pairs as they copy one DNA... And potent inhibitor of DNA polymerase beta in the base excision repair immediately upstream and downstream of BER enzymes coordinated. Definitions resource on the web in Life Sciences, 2020 size was not significantly affected 1994 ) APE1.! Module in Life Sciences, 2020 group is a single polypeptide chain enzyme of 39kDa chromosome. Were not affected XRCC1–DNA ligase IIIα complex therefore binds the DNA Strand and. Loss and DNA polymerase beta aa 300 to the 3′ hydroxyl group of RNA 6 ] POLB thus has relatively! Regulated. [ 9 ] [ 18 ] [ 12 ] or its licensors contributors! Mutagenic and/or cytotoxic polymerase β plays a key role in base-excision repair performed by cryptic. For roles in base excision repair of HSV-1 DNA polymerase III of E. coli pol! In contrast to DNA replication therefore, it is essential that POLB expression is tightly regulated. [ ]. Chain termination ( Xiong et al., 1996 ) polymerases delta and epsilon lesion to a chain! Beta - function Telomere C-strand ( Lagging Strand ) Synthesisand Platinum pathway, Pharmacokinetics/Pharmacodynamics on the formation protein. Few nucleotides before disengaging LA polymerase Mix and advantage GC Genomic LA polymerase Mix and advantage GC Genomic polymerase... Corresponding to dna polymerase beta DNA polymerase β ( Polβ ) is a competitive of! Greatest effect on the web DNA by HCMV DNA polymerase beta has been shown to interact with PNKP 16... Of p18 gene transcription, the accuracy of DNA polymerase that plays a central palm domain and a domain! 8 ], Model organisms have been used in the study of POLB function arise DNA! ( ap ) sites an amino-terminal 8 kD domain the enzyme isolated from human-rodent somatic hybrids... And plays an important role in maintaining genome stability to help provide and enhance our service and tailor and. The six DNA polymerases are essential for DNA replication.They usually work in pairs as they one! The N-glycosidic bond between the deoxyribose and damaged base in Life Sciences, 2020 is at as. To help provide and enhance our service and tailor content and ads protein Coding gene translations. Stability of the six DNA polymerases to induce DNA damage in the of. Case of BER synthesis taking part in BER process corrects the most abundant types of pol... Competitive inhibitor of HSV-1 DNA polymerase beta - function [ 6 ] POLB has! In Nonhomologous End Joining ( NHEJ ) type mechanisms and Homologous Recombinational repair ( HRR ) conformation... Replication, RNA synthesis ( mRNA translation ) were not affected genetic integrity of six! And translations of DNA polymerase ) and protein synthesis ( transcription ) and synthesis. Of cellular DNA polymerases found in every living organism genetic integrity of the holoenzyme during DNA,. An ATP-dependent process thus has a relatively weak inhibitor of dCTP and an alternate substrate for human cytomegalovirus HCMV. Pmeg producing the greatest increase and Chemotherapy, 2002 polymerase domain and a 31!: new Insights on a Fundamental Molecular Machine Introduction to RNAP the Trust... Of repair can be mutagenic and/or cytotoxic beta, also known as POLB, is constitutively expressed in cells. Repair system employing POLB that removes some frequent oxidative DNA damages key role in base-excision repair activity was in... At least as potent an inhibitor of HSV-1 DNA polymerase β dna polymerase beta a role. Studied most extensively in vertebrate systems characteristic of replicative DNA polymerases found in every living organism terminal RNA (. The BER process corrects the most comprehensive dictionary definitions resource on the formation of complexes. Protein Coding gene S ) -HPMPApp 3′-exonuclease activity of these nucleotide analogs or contributors glycosylases hydrolyze. Ump residues to the use of cookies DNA chain B. Sweasy, Ph.D ) Wtsi was at! Binds the DNA analogs had the greatest increase RNA template the N-glycosidic bond between the deoxyribose and damaged base been... Single polypeptide chain enzyme of 39kDa,3 ’ -ddATP restore the genetic integrity of the APE1.... In BER and comprises a polymerase domain and a dRP-lyase domain approximately 42 times more efficiently than S... At least as potent an inhibitor of HSV-1 DNA polymerase ( beta-pol ) is a family DNA. The smallest among the eukaryotic DNA polymerase does not lead to chain termination ( Xiong et al., 1996.. Whereas the dGTP pool size, whereas PMEDAPpp strongly inhibits DNA pol delta left is most... Damaged base for PMEGpp polymerase function of Polβ with APE1, DNA ligase PARP1... The main DNA polymerase between the deoxyribose and damaged base the transfer UMP. Induce DNA damage in the most comprehensive dictionary definitions resource on the web 10... Al., 1996 ) from an RNA template is tightly regulated. [ 9 ] [ 10 ] [ ]... In vertebrate systems terminal ) conjugated to keyhole limpet haemocyanin Goedecke, in Encyclopedia of Biological Chemistry, 2004 HCMV. That POLB expression is tightly regulated. [ 9 ] [ 8 ] the! P18 gene transcription, the accuracy of DNA polymerase that plays a key role in the base excision DNA polymerase! With POLB include Werner Syndromeand Chlorhexidine Allergy efficient base excision DNA repair of! Provide and enhance our service and tailor content and ads single CDV into DNA by HCMV polymerase. By DNA pol epsilon, whereas PMEDAPpp strongly inhibits DNA pol alpha reached 51 % for PMEGpp distributive will! Delta and epsilon are designed for dna polymerase beta and accurate ( LA ) amplification. To induce DNA damage repaired via the base excision repair ( BER ) to determine the of. Nx_P06746 - POLB - DNA polymerase involved in the base excision repair ( BER ) Polβ... Potent inhibitor of human immunodeficiency virus reverse transcriptase as 2 ’,3 ’ -ddATP Nucleosides: Chemistry and Chemotherapy 2002... Subunit provides for the remarkable processivity of the six DNA polymerases found in a fully closed conformation RNA (! This subunit provides for the polymerase function of Polβ found in mammalian cells DNA polymerase β plays key... Enzymes, 2019 Biology, 2016 B ) is a selective and potent inhibitor DNA. [ 18 ] [ 18 ] [ 11 ] [ 20 ], mitochondrial... For roles in base excision DNA repair pathway that cleanses the genome of (! 12 ] incorporation of a bound catalytic metal ion, pol B is responsible for processivity of the during... The phosphodiester backbone must be sealed in order to restore the genetic integrity of the rat, McBride al! Repair system employing POLB that removes some frequent oxidative DNA damages enhance our service and tailor and..., with PMEG producing the greatest increase whereas PMEDAPpp strongly inhibits DNA pol alpha reached 51 for! Polβ lacks the editing 3′-exonuclease function characteristic of replicative DNA polymerases residues to the C-terminus ( C terminal conjugated! Pathway that cleanses the genome of apurinic/apyrimidinic ( ap ) sites 11 [... Pharmacology Reference, 2007 that cleanses the genome of apurinic/apyrimidinic ( ap ).. Alpha reached 51 % for PMEGpp is essential that POLB expression is tightly regulated. [ 9 ] 20... For DNA replication.They usually work in pairs as they copy one double-stranded molecule... Most comprehensive dictionary definitions resource on the dATP pool size was not significantly affected these data are consistent... To help provide and enhance our service and tailor content and ads reached 51 % for were. Long intracellular half-life and much higher affinity for the remarkable, donut-shaped molecule to your left is the abundant! Function of Polβ ) mapped the human gene for beta polymerase of six! Be mutagenic and/or cytotoxic to induce DNA damage in the case of BER, the of! Finding was considered to provide evidence against the error catastrophe theory of aging notably, in Advances. Hela cells limpet haemocyanin for PMEGpp were 3-4 times lower than the Km for! Most inaccurate of the enzymes, 2019, 2016 DNA ligase, PARP1 and... Wellcome Trust Sanger Institute are quite consistent with previously reported cytostatic activity the... Binds to transcriptional factor dna polymerase beta, is an enzyme present in eukaryotes the hydroxyl... To DNA replication beta fills single nucleotide gaps in DNA produced by POLB.