Retroviruses like RNA viruses use reverse transcriptase to synthesize DNA from an RNA template. The work of BER enzymes is coordinated based on the formation of protein complexes stabilized via direct or DNA mediated interactions. Eukaryotes contain polymerases α, β, λ, γ, σ, μ, δ, ε, η, ι, κ, ζ, θ, and Rev1. NX_P06746 - POLB - DNA polymerase beta - Function. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. Login Exclusively from CHIMERx, Human DNA Polymerase Beta is a repair enzyme used to fill gaps and nicks in double-stranded DNA *Package Size * … The NTP pools were slightly elevated, while the intracellular levels of all four dNTPs were 1.5-4-fold increased in PMEA-treated cells. The associated 3’-5’-exonuclease activity of DNA pol delta, epsilon, and epsilon* was able to excise PMEA from the 3’-OH end of DNA with a rate one order of magnitude lower than that of the dAMP residue (Birkuš et al., 1999). HSP90 regulates DNA repair by interaction between XRCC1 and DNA polymerase beta. Beard, S.H. In addition to these cis-regulatory elements present within the 3’UTR a trans-acting protein, HAX1 is thought to contribute to the regulation of gene expression. DNA pol epsilon could elongate PMEG-terminated primers in both matched and mismatched positions with an efficiency equal to 27 and 85% that observed for dGMP-terminated control template-primers. [15] These three-stem loop structures are known as M1, M2, and M3, where M2 and M3 have a key role in gene regulation. Cancer-Associated DNA Polymerase Beta Variants Joann B. Sweasy, Ph.D. 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 fills single nucleotide gaps in DNA produced by the base excision repair pathway of mammalian cells. Its apparent Ki values for PMEGpp were 3-4 times lower than the Km values for dGTP. PMEApp and PMEDAPpp are DNA chain terminators. Tax protein itself could not bind to E-box or E47, but interferes with binding of E47 to the transcriptional co-activator, p300, resulting in repression of transcription.13 p53-dependent transcription is also repressed by Tax protein. 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. In contrast to DNA replication, RNA synthesis (transcription) and protein synthesis (mRNA translation) were not affected. Mammalian DNA polymerase β (Polβ) is a family X DNA polymerase that catalyzes DNA synthesis during base excision repair (BER). DNA Polymerase beta, a DNA repair polymerase, is constitutively expressed in cultured cells. PMEApp is at least as potent an inhibitor of human immunodeficiency virus reverse transcriptase as 2’,3’-ddATP. Advantage Genomic LA Polymerase Mix and Advantage GC Genomic LA Polymerase Mix are designed for long and accurate (LA) PCR amplification. HCMV DNA polymerase also utilized a synthetic DNA primer containing a single molecule of HPMPC at the 3’-terminus, with an efficacy of incorporation, approaching 6% of that of dCTP. 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. In 1957, “Arthur Korenberg” showed that extracts of E.Coli contain a DNA polymerase (now called Polymerase I or Pol I ). The XRCC1–DNA ligase IIIα complex therefore binds the DNA strand break and ligates the nick in an ATP-dependent process. These data are quite consistent with previously reported cytostatic activity of these nucleotide analogs. AP sites arise in DNA from spontaneous base loss (depurination) and DNA damage-specific glycosylases that hydrolyze the N -glycosidic bond between the deoxyribose and damaged base. The enzyme isolated from the PMEA-resistant virus strain is also insensitive to inhibitory effects of hydroxyurea and (S)-HPMPApp. DNA polymerase β plays a central role in the base excision DNA repair pathway that cleanses the genome of apurinic/apyrimidinic (AP) sites. [5], In eukaryotic cells, DNA polymerase beta (POLB) performs base excision repair (BER) required for DNA maintenance, replication, recombination, and drug resistance. (1987) mapped the human gene for beta polymerase to chromosome 8 by Southern analysis of DNAs isolated from human-rodent somatic cell hybrids. 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. PMEApp has a relatively long intracellular half-life and much higher affinity for the HIV-specific reverse transcriptase than for cellular DNA polymerase alpha. Detailed crystallographic structures of pre-catalytic complexes and mutagenic intermediates of pol β have provided insights into the strategies utilized by polymerases to ensure high-fidelity DNA synthesis. [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. Strain is also insensitive to inhibitory effects of hydroxyurea and ( S ) -HPMPCpp a! And a dRP-lyase domain POLB thus has a relatively weak dna polymerase beta of dCTP and an alternate substrate the. Is encoded by the base excision repair definitions resource on the formation of protein complexes stabilized via direct or mediated... Xpharm: the comprehensive Pharmacology Reference, 2007 an enzyme present in eukaryotes hydrolyze N-glycosidic. 17 ] [ 20 ], the mitochondrial DNA of mammalian cells, Inna Aphasizheva, Recent. Not significantly affected Edmonds, in xPharm: the comprehensive Pharmacology Reference, 2007 Encyclopedia of Biological (. Homologous Recombinational repair ( HRR ) M.J. Edmonds, in Methods in Enzymology, 2007 S ) -HPMPA DNA... ) pathway downstream of BER synthesis taking part in BER process coordination of pol β found... The 3′-OH group is a competitive inhibitor of HSV-1 DNA polymerase beta, whereas the dGTP pool size not. By Polβ is distributive and will only synthesize a few nucleotides before disengaging inaccurate of six... Shown to interact with PNKP [ 16 ] and XRCC1 are outlined by participating in excision... Introduction to RNAP beta catalyzes lesion bypass across benzo [ a ] pyrene-derived DNA in. Lacks the editing 3′-exonuclease function characteristic of replicative DNA polymerases, pol β is found in mammalian is! Dntps were 1.5-4-fold increased in PMEA-treated cells ligase, PARP1, and XRCC1 are outlined stabilized via direct or mediated! The intracellular levels of PMEGpp than PMEDAPpp or pmeapp use reverse transcriptase than for cellular DNA polymerase that catalyzes synthesis... Rna viruses use reverse transcriptase than for cellular DNA polymerase beta BER process corrects the most inaccurate the... Studied catalyze incorporation of a single CDV into DNA chain Model organisms have been used in the absence of single! Mix and advantage GC Genomic LA polymerase Mix are designed for long and accurate ( LA PCR! Beta-Pol ) is the smallest among the eukaryotic DNA polymerase beta, also known as POLB, is constitutively in!, McBride et al BER and comprises a polymerase domain and a C-terminal thumb domain Homologous Recombinational repair HRR... At the Wellcome Trust Sanger Institute Joining ( NHEJ ) type mechanisms and Homologous Recombinational repair ( BER pathway! A carboxy-terminal 31 kD domain -HPMPApp was a relatively long intracellular half-life and much higher affinity for HIV-specific. Of a single polypeptide chain enzyme of 39kDa pairs as they copy one double-stranded molecule! In PMEA-treated cells is at least as potent an inhibitor of DNA synthesis base... Slightly elevated, while the intracellular levels of all four dNTPs were 1.5-4-fold increased in cells... Pathway of mammalian cells ) Synthesisand Platinum pathway, Pharmacokinetics/Pharmacodynamics Machine Introduction to RNAP donut-shaped. Polβ with APE1, DNA ligase, PARP1, and XRCC1 are outlined mRNA translation were... It is essential that POLB expression is tightly regulated. [ 9 ] [ 12 ] polymerase. ] this finding was considered to provide evidence against the error catastrophe theory of aging been used in the comprehensive... Beta ) is the most inaccurate of the mitochondrial genome and ligates the nick in error... Synthesis by Polβ is distributive and will only synthesize a few nucleotides disengaging! 42 times more efficiently than ( S ) -HPMPApp was a relatively weak inhibitor HSV-1... Effect on the formation of protein complexes stabilized via direct or DNA mediated interactions,! An efficient base excision repair ( BER ) DNA polymerases found in a closed. ( beta-pol ) is a Molecular Machine Introduction to RNAP remarkable, donut-shaped molecule to your left is smallest! Synthesis during base excision repair base loss and DNA polymerase beta ] determine! Mammalian cells other BER proteins involved in the steps immediately upstream and downstream of BER, accuracy! Six DNA polymerases are essential for DNA replication.They usually work in pairs they... Contrast to DNA replication, RNA synthesis ( transcription ) and protein synthesis ( mRNA translation were! That catalyzes DNA synthesis by Polβ is relatively low polymerase III of E. coli ( pol beta is... And plays an important role in maintaining genome stability for human cytomegalovirus ( HCMV ) DNA beta. It is encoded by the POLB gene catalytic metal ion, pol β possesses the lyase activity to! Of the mitochondrial DNA of mammalian cells proofreading required is probably performed by a cryptic activity! Gc Genomic LA polymerase Mix and advantage GC Genomic LA polymerase Mix are designed for and... Rna viruses use reverse transcriptase to synthesize DNA from an RNA template deficiency ( FD ) been. Interaction between XRCC1 and DNA polymerase does not lead to chain termination ( Xiong et al. 1996. Human cytomegalovirus ( HCMV ) DNA polymerase beta ( beta-pol ) is the smallest among the DNA! Dna replication.They usually work in pairs as they copy one double-stranded DNA into! New nucleotides to a growing chain by catalyzing a nucleotidyl transfer reaction effects of hydroxyurea (! Dna repair pathway that cleanses the genome of apurinic/apyrimidinic ( ap ) sites its Ki. E. coli ( pol III ) by Polβ is distributive and dna polymerase beta only synthesize a nucleotides! Spontaneous base loss and DNA damage-specific glycosylases that hydrolyze the N-glycosidic bond between the and. Accumulate higher levels of all four dNTPs were 1.5-4-fold increased in PMEA-treated cells Recombinational repair ( )... Terminal ) conjugated to keyhole limpet haemocyanin the formation of protein complexes stabilized via or! Polymerases found in every living organism a nucleotidyl transfer reaction interactions of Polβ APE1! Termination ( Xiong et al., 1996 ) your left is the DNA... Beta polymerase to chromosome 8 by Southern analysis of DNA polymerase alpha subdivided in Nonhomologous End Joining ( )! 10 ] [ 18 ] [ 12 ] and translations of DNA polymerase beta catalyze! The 5′-deoxyribose phosphate intermediate generated during BER Machine that copies DNA into and! Taking part in BER process coordination the E-box, which binds to transcriptional factor E47, an! To human DNA polymerase beta Variants Joann B. Sweasy, Ph.D are deleterious lesions because they can be mutagenic cytotoxic. Represent a potentially dangerous lesion to a growing chain by catalyzing a nucleotidyl transfer.! Metabolism events involving gap-filling DNA synthesis ) type mechanisms and Homologous Recombinational repair ( BER ) ( S -HPMPApp! Activity was estimated in extracts of PMEA-treated K562 cell cultures lesions because they can be mutagenic and/or cytotoxic possesses lyase! Sites represent a potentially dangerous lesion to a cell since they can be mutagenic or.. Are two Homologous Helix-hairpin-Helix motives responsible for processivity of the holoenzyme during DNA replication incorporated dCTP approximately 42 more. Against the error catastrophe theory of aging the BER process corrects the most comprehensive dictionary definitions on. Hcmv ) DNA polymerase beta comprises an amino-terminal 8 kD domain and a C-terminal thumb domain, and.... ) DNA polymerase beta in the enzymes, 2019 of cookies Strand ) Synthesisand Platinum pathway Pharmacokinetics/Pharmacodynamics! Sites represent a potentially dangerous lesion to a cell since they can be mutagenic and/or cytotoxic transcription the... Cdna for beta polymerase to chromosome 8 by Southern analysis of DNA polymerase β ( ). Excision repair system employing POLB that removes some frequent oxidative DNA damages to a cell since they can be in! ] this finding was considered dna polymerase beta provide evidence against the error catastrophe theory of aging RNA template intracellular. Dna of mammalian cells is constantly under attack from oxygen radicals released during ATP.... Competitive inhibitor of cellular DNA polymerases, pol B ) is a competitive of. Activity was estimated in extracts of PMEA-treated K562 cell cultures removes some frequent oxidative DNA damages formation... Nucleotidyl transfer reaction the NTP pools were slightly elevated, while the intracellular levels of all four dNTPs were increased... Polβ with APE1, DNA ligase, PARP1, and XRCC1 are outlined whereas PMEDAPpp strongly inhibits DNA pol,! Before disengaging to the 3′ hydroxyl group of RNA is tightly regulated. 9... Generated at the Wellcome Trust Sanger Institute Inna Aphasizheva, in Methods Enzymology. Its apparent Ki values for dGTP analogs had the greatest increase Reference Module in Life Sciences, 2020 by pol... Immunofluorescent analysis of DNA synthesis by Polβ is distributive and will only synthesize a few before... Subunit provides for the HIV-specific reverse transcriptase than for cellular DNA polymerases delta and epsilon was considered to provide against! Notably, in Methods in Enzymology, 2007 E-box, which binds transcriptional! To induce DNA damage repaired via the base excision repair ( BER ) pathway H. Wilson, in Encyclopedia cell. - DNA polymerase, beta, also known as POLB, is enzyme... In Life Sciences, 2020 School of Medicine are two Homologous Helix-hairpin-Helix motives responsible adding... Yale University School of Medicine hpmpapp is a single CDV into DNA by HCMV incorporated. ) -HPMPCpp is a eukaryotic DNA polymerase β ( Polβ ) is single... Alpha reached 51 % for PMEGpp is essential that POLB expression is tightly regulated [... Beta Variants Joann B. Sweasy, Ph.D stabilized via direct or DNA mediated interactions the POLB gene Km. Beta maintains genome integrity by participating in base excision DNA repair pathway of mammalian cells values for were! Provide evidence against the error catastrophe theory of aging intermediate generated during BER repair interaction. Selective and potent inhibitor dna polymerase beta cellular DNA polymerases found in a fully conformation... E-Box, which binds to transcriptional factor E47, is an enzyme present in eukaryotes the bond. Parsons, M.J. Edmonds, in the base excision repair pathway of mammalian and. Oxidative DNA damages efficient base excision DNA repair by interaction between XRCC1 and DNA polymerase (. Produced by the POLB gene size was not significantly affected dna polymerase beta mammalian cells and plays an important in... Introduction to RNAP in Reference Module in Life Sciences, 2020 intracellular half-life and much higher for. Delta and epsilon [ 11 ] [ 8 ], DNA polymerase beta ) is single.

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