3'–5'-exonuclease, ABO4/POL2a/TIL1, Afu polymerase, ASFV DNA polymerase, ASFV Pol X, B-family replicative DNA polymerase, beta type DNA polymerase, Bst DNA polymerase, CpDNApolI, DBH, Dbh DNA polymerase, Dbh polymerase, ddNTP-sensitive DNA polymerase, Deep Vent DNA polymerase, DeepVent DNA polymerase, deoxynucleate polymerase, deoxyribonucleate nucleotidyltransferase, deoxyribonucleic acid duplicase, deoxyribonucleic acid polymerase, deoxyribonucleic duplicase, deoxyribonucleic polymerase, deoxyribonucleic polymerase I, DinB DNA polymerase, DinB homologue, Dmpol zeta, DNA deoxynucleotidyltransferase, DNA duplicase, DNA nucleotidyltransferase, DNA nucleotidyltransferase (DNA-directed), DNA pol, DNA pol B1, DNA Pol eta, DNA Pol lambda, DNA pol NI, DNA pol Y1, DNA polmerase beta, DNA polymerase, DNA polymerase 1, DNA polymerase 2, DNA polymerase 4, DNA polymerase A, DNA polymerase alpha, DNA polymerase B, DNA polymerase B1, DNA polymerase B2, DNA polymerase B3, DNA polymerase beta, DNA polymerase D, DNA polymerase Dbh, DNA polymerase delta, DNA polymerase Dpo4, DNA polymerase epsilon, DNA polymerase eta, DNA polymerase gamma, DNA polymerase I, DNA polymerase II, DNA polymerase III, DNA polymerase III epsilon subunit, DNA polymerase iota, DNA polymerase IV, DNA polymerase kappa, DNA polymerase lambda, DNA polymerase mu, DNA polymerase ny, DNA polymerase pyrococcus kodakaraensis, DNA polymerase theta, DNA polymerase V, DNA polymerase X, DNA polymerase zeta, DNA polymerases B, DNA polymerases D, DNA polymmerase I, DNA primase-polymerase, DNA replicase, DNA replication polymerase, DNA-dependent DNA polymerase, DNAP, DP1Pho, DP2Pho, Dpo1, Dpo2, Dpo3, Dpo4, Dpo4 polymerase, Dpo4-like enzyme, duplicase, error-prone DNA polymerase, error-prone DNA polymerase X, family B-type DNA polymerase, hoPolD, HSV 1 POL, Igni_0062, K4 polymerase, K4pol, K4PolI, kDNA replication protein, KDO XL DNA polymerase, KF(exo-), KF-, Klenow fragment, Klenow-like DNA polymerase I, KOD DNA polymerases, lesion-bypass DNA polymerase, M1 DNA polymerase, M1pol, MacDinB-1, MA_4027, Miranda pol beta protein, mitochondrial DNA polymerase, Mka polB, More, MsDpo4, mtDNA polymerase NI, mtDNA replicase, Neq DNA polymerase, non-replicative DNA polymerase III, nucleotidyltransferase, deoxyribonucleate, OsPOLP1, PabPol D, PabpolB, PabpolD, Pfu, Pfu DNA polymerase, Pfu Pol, Pfu-POl, PH0121, PH0123, phi29 DNA polymerase, phi29 DNApol, PhoPolD, phPol D, Pol, pol alpha, Pol B, Pol B1, pol beta, Pol BI, pol delta, pol E, POl epsilon, Pol eta, Pol gamma, Pol I, Pol II, pol III, pol iota, Pol IV, pol kappa, pol kappaDELTAC, Pol lambda, Pol mu, pol NI, Pol ny, Pol theta, Pol V, pol Vent (exo-), Pol X, Pol zeta, Pol-beta, POL1, Pol2, POL2a, Pol3, Pol31, PolB, POlB1, polbeta, polD, POLD4, Poldelta, POLdelta1, PolDPho, Polepsilon, Poleta, POLG, PolH, polI, POLIB, POLIC, POLID, poliota, Polkappa, PolX, PolY, poly iota, polymerase alpha catalytic subunit A, polymerase III, pORF30, Pwo DNA polymerase, R2 polymerase, R2 reverse transcriptase, R2-RT, RAD30, RB69 DdDp, RB69 DNA Polymerase, RB69pol, Rec1, repair polymerase, replicative DNA polymerase, reverse transcriptase, RKOD DNA polymerase, Rv1537, Rv3056, Saci_0554, sequenase, Sso, Sso DNA pol B1, Sso DNA pol Y1, Sso DNA polymerase Y1, Sso DNApol, Sso pol B1, SSO0552, SSO2448, SsoDpo1, SsoPolB1, SsoPolY, Szi DNA polymerase, T4 DNA polymerase, T7 DNA polymerase, Taq DNA polymerase, Taq Pol I, Taq polymerase, Tba5 DNA polymerase, Tca DNA polymerase, Tga PolB, TGAM_RS07365, Tkod-Pol, translesion DNA polymerase, translesion DNA synthesis polymerase, translesion polymerase Dpo4, UL30/UL42, UmuD'2C, UmuD'2C-RecA-ATP, Vent polymerase, X family DANN polymerase, Y-family DNA polymerase eta
x * 140000 (alpha) + x * 25000 (epsilon) + x * 10000 (theta), pol III, can repair short gaps created by nuclease in duplex DNA, for efficient replication of the long, single-stranded templates pol III requires auxiliary subunits beta MW 37000, gamma MW 52000, and delta MW 32000
DNA polymerase alpha is composed of: 1. a cluster of related high-molecular-weight polypeptides predominantly of 165000-180000 MW containing the catalytic function, 2. a polypeptide of 70000 MW with unknown catalytic function, 3. two polypeptides of 55000-60000 and 48000-49000 associated with primase activity
the human DNA polymerase epsilon holoenzyme is comprised of the catalytic p261 subunit and the noncatalytic p59, p17, and p12 small subunits. The presence of the p261 C-terminal domain (p261C) and the three small subunits increased the DNA binding affinity and the base substitution fidelity
heterotetramer consisting of two small subunits (locus name: PH0123) and two large subunits (locus name: PH0121). The large subunits is the catalytic subunit of DNA polymerase, while the small subunits is the catalytic subunit of Mre11-like 3'-5' exonuclease
heterotetramer consisting of two small subunits (locus name: PH0123) and two large subunits (locus name: PH0121). The large subunits is the catalytic subunit of DNA polymerase, while the small subunits is the catalytic subunit of Mre11-like 3'-5' exonuclease
1 * 100000, likely it is cleaved by the action of endogenous proteases during the purification procedure. As a consequence of that, two proteolytic fragments of about 50 and 40 kDa, in addition to the intact 100-kDa molecular species, can be detected upon SDS-PAGE
the enzyme is able to physically associate with itself to form a trimer. This complex is stabilized in the presence of DNA. Initially a single DNA polymerase binds to DNA followed by the cooperative binding of two additional molecules of the polymerase at higher concentrations of the enzyme. These are specific polymerase-polymerase interactions and not just separate binding events along DNA. The presence of a trimeric DNA polymerase complex that is able to synthesize long DNA strands more efficiently than the monomeric form
the enzyme is able to physically associate with itself to form a trimer. This complex is stabilized in the presence of DNA. Initially a single DNA polymerase binds to DNA followed by the cooperative binding of two additional molecules of the polymerase at higher concentrations of the enzyme. These are specific polymerase-polymerase interactions and not just separate binding events along DNA. The presence of a trimeric DNA polymerase complex that is able to synthesize long DNA strands more efficiently than the monomeric form
multipolypeptide complex in prokaryotes and eukaryotes, three structural levels can be distinguished: 1. core polymerase (responsible for basic polymerization step), 2. DNA polymerase holoenzyme (composed of the core polymerase, which is responsible for the basic polymerization step and associated accessory proteins, a complex which is fully active on naturally occuring DNA templates), 3. holoenzyme embedded in a higher order structure, such as an asymmetric dimer or other complex which acts in concert with other known replication enzymes
multipolypeptide complex in prokaryotes and eukaryotes, three structural levels can be distinguished: 1. core polymerase (responsible for basic polymerization step), 2. DNA polymerase holoenzyme (composed of the core polymerase, which is responsible for the basic polymerization step and associated accessory proteins, a complex which is fully active on naturally occuring DNA templates), 3. holoenzyme embedded in a higher order structure, such as an asymmetric dimer or other complex which acts in concert with other known replication enzymes
multipolypeptide complex in prokaryotes and eukaryotes, three structural levels can be distinguished: 1. core polymerase (responsible for basic polymerization step), 2. DNA polymerase holoenzyme (composed of the core polymerase, which is responsible for the basic polymerization step and associated accessory proteins, a complex which is fully active on naturally occuring DNA templates), 3. holoenzyme embedded in a higher order structure, such as an asymmetric dimer or other complex which acts in concert with other known replication enzymes
three-dimensional structure prediction using homology modeling. The structure for DNA polymerase domain (residues 471-878) of Gkaue polI is depicted resembling a right hand with fingers, palm, and thumb subdomains
three-dimensional structure prediction using homology modeling. The structure for DNA polymerase domain (residues 471-878) of Gkaue polI is depicted resembling a right hand with fingers, palm, and thumb subdomains
the holoenzyme of pol gamma consists of a catalytic subunit and a dimeric form of its accessory subunit. The catalytic subunit is a 140 kDa enzyme, i.e. p140, that contains an N-terminal exonuclease domain connected by a linker region to a C-terminal polymerase domain and has DNA polymerase, 3'->5' exonuclease and 5' dRP lyase activities. The accessory subunit is a 55 kDa protein, i.e. p55, required for tight DNA binding and processive DNA synthesis
Dpo4 has a spacious, highly solvent-accessible active-site region, schematic and molecular surface representations of Dpo4 ternary structure, comparison to the high-fidelity DNA polymerase Bacillus fragment, overview
Dpo4 has a spacious, highly solvent-accessible active-site region, schematic and molecular surface representations of Dpo4 ternary structure, comparison to the high-fidelity DNA polymerase Bacillus fragment, overview
investigation of the structure of the recombinant enzyme in the free and DNA-bound states by limited proteolysis experiments and fluorescence quenching measurements
solution-phase NMR study, assignments for the backbone nitrogen, carbon, and amide proton NMR signals of the catalytic core of the enzyme consisting of the finger, palm, and thumb domains