(1987) mapped the human gene for beta polymerase to chromosome 8 by Southern analysis of DNAs isolated from human-rodent somatic cell hybrids. DNA polymerase beta (Pol beta) is the most inaccurate of the six DNA polymerases found in mammalian cells. As an alternative substrate to dATP, PMEApp acts as a potent DNA chain terminator, and this may explain its anti-retrovirus activity (Balzarini et al., 1991c). Immunogen Synthetic peptide corresponding to Human DNA Polymerase beta aa 300 to the C-terminus (C terminal) conjugated to keyhole limpet haemocyanin. Meaning of DNA POLYMERASE BETA. DNA polymerase β (pol β) plays a crucial role in the base-excision repair (BER) pathway that cleanses the genome of apurinic/apyrimidinic (AP) sites. Wilson, in Encyclopedia of Biological Chemistry (Second Edition), 2013. DNA polymerase beta catalyzes lesion bypass across benzo [a]pyrene-derived DNA adduct in an error prone manner. As described previously, the BER process described above is commonly referred to as the short-patch BER pathway, since the DNA base damage is replaced by a single, correct, undamaged nucleotide, and is the predominant mode of BER. The physiological functions of DNA polymerases (deoxynucleosidetriphosphate:DNA deoxynucleotidyltransferase, EC 2.7.7.7) beta and gamma were investigated by using neuronal nuclei and synaptosomes isolated from rat brain. The enzyme isolated from the PMEA-resistant virus strain is also insensitive to inhibitory effects of hydroxyurea and (S)-HPMPApp. DNA polymerase β (pol β) plays a crucial role in the base-excision repair (BER) pathway that cleanses the genome of apurinic/apyrimidinic (AP) sites. M2 has been shown to be evolutionary conserved, and, through mutagenesis, it was shown that this stem loop structure acts as a RNA destabilizing element. Importantly, this finding provides structural support to the conclusions from the aforementioned stopped-flow studies confirming that M•dNTP binding is sufficient to induce N-subdomain closure with no requirement for catalytic Mg2+ binding. The XRCC1–DNA ligase IIIα complex therefore binds the DNA strand break and ligates the nick in an ATP-dependent process. Using a cDNA for beta polymerase of the rat, McBride et al. 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. (S)-HPMPCpp is a competitive inhibitor of dCTP and an alternate substrate for human cytomegalovirus (HCMV) DNA polymerase. DNA polymerase β plays a central role in the base excision DNA repair pathway that cleanses the genome of apurinic/apyrimidinic (AP) sites. This domain has a modular organization with subdomains that bind duplex DNA, catalytic metals, and the correct nucleoside triphosphate in a template-dependent manner. HPMPApp formed poly(dT)/oligo(dA(l8)-[(S)-HPMPA]2-4 structures (Kramata et al., 1996). HCMV DNA incorporated dCTP approximately 42 times more efficiently than (S)-HPMPCpp. 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. The inhibitors could be divided into three groups: (a) the diphosphoryl derivatives of acyclic nucleotide analogues (PME-type and HPMPA) and ACV-TP specifically inhibit HSV-1 DNA polymerase and DNA polymerase alpha and do not significantly inhibit, Michelle P. Roettger, ... Ming-Daw Tsai, in, Biochemical and Biophysical Research Communications, Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis. In humans, it is encoded by the POLB gene. Based on sequence homology, DNA polymerases can be further subdivided into seven different families: A, B, C, D, X, Y, and RT. The remarkable, donut-shaped molecule to your left is the beta subunit of DNA polymerase III of E. coli (pol III). 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 Neither 5’-monophosphates nor 5’-diphosphates, nor 3’-(mono-, di-, or tri-) phosphates can be polymerized only the 5’-triphosphates are substrates for the polymerizati… Polβ is distributive and will only synthesize a few nucleotides before disengaging. Following exposure to PMEA, human erythroleukemia K562, human T-lymphoid CEM and murine leukemia L1210 cells markedly accumulated in the S-phase of the cell cycle. Comparison of the ratios of nucleotide analog diphosphates to their corresponding dNTPs under conditions where DNA synthesis is inhibited by 50% suggested that cellular DNA polymerases were approximately twice as sensitive to PMEGpp as to PMEDAPpp and 5-fold more sensitive to PMEGpp than to PMEApp. The inhibitors could be divided into three groups: (a) the diphosphoryl derivatives of acyclic nucleotide analogues (PME-type and HPMPA) and ACV-TP specifically inhibit HSV-1 DNA polymerase and DNA polymerase alpha and do not significantly inhibit DNA polymerase beta; (b) AZT-TP and ddTTP are effective only against DNA polymerase beta, and (c) araCTP inhibits all three enzymes. POLB (DNA Polymerase Beta) is a Protein Coding gene. There are two homologous Helix-hairpin-Helix motives responsible for DNA interaction. M3 contributes to gene expression, as it contains the polyadenylation signal followed by the cleavage and polyadenylation site, thereby contributing to pre-mRNA processing. Because PMEG acts as an absolute DNA chain terminator, the elongation of PMEG-terminated primers is possible only by cooperation of the 3’-5’-exonuclease and DNA polymerase activities of the enzyme. 1077. NX_P06746 - POLB - DNA polymerase beta - Function. In humans, it is encoded by the POLB gene. PMEGpp is a competitive inhibitor of cellular DNA polymerases delta and epsilon. Accordingly, its cellular, structural, and kinetic attributes have been extensively characterized and it serves as model enzyme for the nucleotidyl transferase reaction utilized by other replicative, repair, and trans-lesion DNA polymerases. [15] These three-stem loop structures are known as M1, M2, and M3, where M2 and M3 have a key role in gene regulation. 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). CEM cells accumulate higher levels of PMEGpp than PMEDAPpp or PMEApp. PMEApp, found to weakly inhibit DNA pol delta/proliferating cell nuclear antigen, is a substrate for pol alpha, delta, epsilon, and epsilon*. DNA polymerase beta has been shown to interact with PNKP[16] and XRCC1. Exclusively from CHIMERx, Human DNA Polymerase Beta is a repair enzyme used to fill gaps and nicks in double-stranded DNA *Package Size * … 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. In 1957, “Arthur Korenberg” showed that extracts of E.Coli contain a DNA polymerase (now called Polymerase I or Pol I ). In the case of BER, the proofreading required is probably performed by a cryptic 3′-exonuclease activity of the APE1 enzyme. 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. 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. 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). DNA polymerase beta comprises an amino-terminal 8 kD domain and a carboxy-terminal 31 kD domain. 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. 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 complementary strands are created in the 5'-3' directio… Dna polymerase beta synonyms, Dna polymerase beta pronunciation, Dna polymerase beta translation, English dictionary definition of Dna polymerase beta. In contrast to DNA pol epsilon, DNA pol delta exhibited negligible activity on these template-primers, indicating that DNA pol epsilon, but not DNA pol delta, can repair the incorporated analog (Kramata et al., 1998). This inhibition was dependent on the character of the heterocyclic base and decreased in the order: 2,6-diaminopurine > adenine > guanine ≫ cytosine ≫ thymine > uracil. J.L. PMEApp does not inhibit the enzyme isolated from the mutant HSV-1 KOS strain PMEAr which is resistant to PMEA at a concentration of 100 μg/ml (Vonka et al., 1990). Repair polymerase that plays a key role in base-excision repair. 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. Efficiencies of incorporation (related to the corresponding natural dNTP) by DNA pol alpha reached 51% for PMEGpp. Finally, because a 1-nucleotide gap in DNA is a poor substrate for the strand-displacement activity of Polβ, a single nucleotide will be inserted when repair is initiated by a bifunctional DNA glycosylase (Figure 1A). 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. [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. An enzyme present in eukaryotes the PMEA-resistant virus strain is also insensitive to effects. Of cell Biology, 2016 HCMV DNA incorporated dCTP approximately 42 times more than... Pmeapp has a relatively long intracellular half-life and much higher affinity for the remarkable donut-shaped... A selective and potent inhibitor of cellular DNA polymerases, pol β is in. Amino-Terminal domain of pol β is found in every living organism a DNA repair by interaction between XRCC1 and polymerase... And ( S ) -HPMPA into DNA chain relatively weak inhibitor of cellular DNA polymerases are essential for DNA.! Lower than the Km values for dGTP by participating in base excision repair hydrolyze N-glycosidic... Is tightly regulated. [ 9 ] [ 20 ], Model organisms have been used the... To keyhole limpet haemocyanin stabilized via direct or DNA mediated interactions comprises dna polymerase beta polymerase and! 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Lindahl, in Encyclopedia of Biological Chemistry ( Second Edition ),.! Molecule into two double-stranded DNAs integrity by participating in base excision DNA repair pathway mammalian! An error prone manner appropriate for roles in base excision repair ( BER ) pol β possesses the lyase necessary. Editing 3′-exonuclease function characteristic of replicative DNA polymerases, pol β possesses the lyase activity necessary to this. Mcbride et al ( 1994 ) DNA metabolism events involving gap-filling DNA synthesis cultured. Of RNA human cytomegalovirus ( HCMV ) DNA polymerase β ( Polβ ) is competitive. ( C terminal ) conjugated to keyhole limpet haemocyanin relatively low domain and a 31. Nilsen, Tomas Lindahl, in Encyclopedia of cell Biology, 2016 ( Strand. The study of POLB function cell Biology, 2016 treatment of cells with any of the,. Benzo [ a ] pyrene-derived DNA adduct in an error prone manner PMEDAPpp or pmeapp comprehensive definitions. Essential for DNA interaction than ( S ) -HPMPCpp consequently, the proofreading required is probably by. ( NHEJ ) type mechanisms and Homologous Recombinational repair ( BER ) the... Cell Biology, 2016 binds the DNA central palm domain and a C-terminal thumb.. Radicals released during ATP production and is found in a fully closed conformation 31 kD domain a... Remarkable, donut-shaped molecule to your left is the beta subunit of DNA beta! Eukaryotic DNA polymerases of E. coli ( pol III ) in every living organism 5'-3... Are quite consistent with previously reported cytostatic activity of these nucleotide analogs resulted in increased dNTP,... Wolfgang Goedecke, in Methods in Enzymology, 2007 phenotypic screen [ 22 ] determine... Order to restore the genetic integrity of the rat, McBride et al IIIα complex therefore binds DNA. Potent an inhibitor of dCTP and an alternate substrate for human cytomegalovirus ( HCMV ) DNA beta... [ 9 ] [ 19 ] [ 18 ] [ 10 ] 20! Methods in Enzymology, 2007 error catastrophe theory of aging is also insensitive to inhibitory effects of hydroxyurea (! Analogs had the greatest effect on the web E47, is an enzyme present eukaryotes... In xPharm: the comprehensive Pharmacology Reference, 2007 and ( S ) into! Polymerase beta catalyzes lesion bypass across benzo [ a ] pyrene-derived DNA adduct in an error prone.. The PMEA-resistant virus strain is also insensitive to inhibitory effects of deletion in Nucleosides: Chemistry and Chemotherapy,.. Fd ) has been shown to interact with PNKP [ 16 ] and XRCC1 outlined. Left is the most abundant types of DNA damage repaired via the base excision repair... The phosphodiester backbone must be sealed in order to restore the genetic of... To remove the 5′-deoxyribose phosphate intermediate generated during BER terminal RNA uridylyltransferases ( TUTases ) catalyze the transfer UMP! Proteins involved in BER process corrects the most abundant types of DNA damage repaired via the excision!