Relevant bibliographies by topics / DNA polymerases

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'DNA polymerases'

Author: Grafiati
Published: 4 June 2021
Last updated: 31 July 2024

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Journal articles on the topic "DNA polymerases"

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Jung, G. H., M. C. Leavitt, J. C. Hsieh, and J. Ito. "Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases." Proceedings of the National Academy of Sciences 84, no. 23 (December 1, 1987): 8287–91. http://dx.doi.org/10.1073/pnas.84.23.8287.

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Walsh, Jason M., and Penny J. Beuning. "Synthetic Nucleotides as Probes of DNA Polymerase Specificity." Journal of Nucleic Acids 2012 (2012): 1–17. http://dx.doi.org/10.1155/2012/530963.

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The genetic code is continuously expanding with new nucleobases designed to suit specific research needs. These synthetic nucleotides are used to study DNA polymerase dynamics and specificity and may even inhibit DNA polymerase activity. The availability of an increasing chemical diversity of nucleotides allows questions of utilization by different DNA polymerases to be addressed. Much of the work in this area deals with the A family DNA polymerases, for example,Escherichia coliDNA polymerase I, which are DNA polymerases involved in replication and whose fidelity is relatively high, but more recent work includes other families of polymerases, including the Y family, whose members are known to be error prone. This paper focuses on the ability of DNA polymerases to utilize nonnatural nucleotides in DNA templates or as the incoming nucleoside triphosphates. Beyond the utility of nonnatural nucleotides as probes of DNA polymerase specificity, such entities can also provide insight into the functions of DNA polymerases when encountering DNA that is damaged by natural agents. Thus, synthetic nucleotides provide insight into how polymerases deal with nonnatural nucleotides as well as into the mutagenic potential of nonnatural nucleotides.
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Peramachi Palanivelu. "Identification of Polymerase and Proofreading Exonuclease Domains in the DNA Polymerases IA, IB and Nuclear-Encoded RNA Polymerase of the Plant Chloroplasts." World Journal of Advanced Research and Reviews 17, no. 3 (March 30, 2023): 706–27. http://dx.doi.org/10.30574/wjarr.2023.17.3.0455.

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Chloroplast plays a crucial role in all photosynthetic plants and converts the light energy to chemical energy. It is a semi-autonomous organelle and is mostly controlled by its own genome and partly by the nuclear imports. To replicate its own genome, it uses two DNA polymerases, viz. polymerases IA and IB. DNA polymerase IA showed 72.45% identity to polymerase IB, but only 35.35% identity to the E. coli DNA polymerase I. Multiple sequence alignment (MSA) analysis have shown that the DNA polymerases IA and IB and the E. coli DNA polymerase I possess almost identical active sites for polymerization and proofreading (PR) functions, suggesting their possible common evolutionary origin. The nuclear-encoded RNA polymerase (NEP) is imported from the nucleus and involves in the transcription of all the four subunits of the chloroplast RNA polymerase. The polymerase catalytic core of the DNA polymerases IA, IB and the NEP are remarkably conserved and is in close agreement with other DNA/RNA polymerases reported already, and possess a typical template-binding pair (-YG-), a basic catalytic amino acid (K) to initiate catalysis and a basic nucleotide selection amino acid R at -4 from K. The DNA polymerases IA and IB are very similar to prokaryotic DNA polymerases, except in possessing a zinc-binding motif (ZBM) in them, like the eukaryotic replicases. Interestingly, the PR exonucleases of all three polymerases belong to the DEDD-superfamily of exonucleases. The DNA polymerases IA and IB belong to the DEDD(Y)-subfamily, whereas the NEP belongs to the DEDD(H)-subfamily.
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Raia, Pierre, Marc Delarue, and Ludovic Sauguet. "An updated structural classification of replicative DNA polymerases." Biochemical Society Transactions 47, no. 1 (January 15, 2019): 239–49. http://dx.doi.org/10.1042/bst20180579.

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AbstractReplicative DNA polymerases are nano-machines essential to life, which have evolved the ability to copy the genome with high fidelity and high processivity. In contrast with cellular transcriptases and ribosome machines, which evolved by accretion of complexity from a conserved catalytic core, no replicative DNA polymerase is universally conserved. Strikingly, four different families of DNA polymerases have evolved to perform DNA replication in the three domains of life. In Bacteria, the genome is replicated by DNA polymerases belonging to the A- and C-families. In Eukarya, genomic DNA is copied mainly by three distinct replicative DNA polymerases, Polα, Polδ, and Polε, which all belong to the B-family. Matters are more complicated in Archaea, which contain an unusual D-family DNA polymerase (PolD) in addition to PolB, a B-family replicative DNA polymerase that is homologous to the eukaryotic ones. PolD is a heterodimeric DNA polymerase present in all Archaea discovered so far, except Crenarchaea. While PolD is an essential replicative DNA polymerase, it is often underrepresented in the literature when the diversity of DNA polymerases is discussed. Recent structural studies have shown that the structures of both polymerase and proofreading active sites of PolD differ from other structurally characterized DNA polymerases, thereby extending the repertoire of folds known to perform DNA replication. This review aims to provide an updated structural classification of all replicative DNAPs and discuss their evolutionary relationships, both regarding the DNA polymerase and proofreading active sites.
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Hałas, A., A. Ciesielski, and J. Zuk. "Involvement of the essential yeast DNA polymerases in induced gene conversion." Acta Biochimica Polonica 46, no. 4 (December 31, 1999): 862–72. http://dx.doi.org/10.18388/abp.1999_4107.

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In the yeast Saccharomyces cerevisiae three different DNA polymerases alpha, delta and epsilon are involved in DNA replication. DNA polymerase alpha is responsible for initiation of DNA synthesis and polymerases delta and epsilon are required for elongation of DNA strand during replication. DNA polymerases delta and epsilon are also involved in DNA repair. In this work we studied the role of these three DNA polymerases in the process of recombinational synthesis. Using thermo-sensitive heteroallelic mutants in genes encoding DNA polymerases we studied their role in the process of induced gene conversion. Mutant strains were treated with mutagens, incubated under permissive or restrictive conditions and the numbers of convertants obtained were compared. A very high difference in the number of convertants between restrictive and permissive conditions was observed for polymerases alpha and delta, which suggests that these two polymerases play an important role in DNA synthesis during mitotic gene conversion. Marginal dependence of gene conversion on the activity of polymerase epsilon indicates that this DNA polymerase may be involved in this process but rather as an auxiliary enzyme.
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Cooper, Christopher D. O. "Archaeal DNA polymerases: new frontiers in DNA replication and repair." Emerging Topics in Life Sciences 2, no. 4 (November 14, 2018): 503–16. http://dx.doi.org/10.1042/etls20180015.

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Archaeal DNA polymerases have long been studied due to their superior properties for DNA amplification in the polymerase chain reaction and DNA sequencing technologies. However, a full comprehension of their functions, recruitment and regulation as part of the replisome during genome replication and DNA repair lags behind well-established bacterial and eukaryotic model systems. The archaea are evolutionarily very broad, but many studies in the major model systems of both Crenarchaeota and Euryarchaeota are starting to yield significant increases in understanding of the functions of DNA polymerases in the respective phyla. Recent advances in biochemical approaches and in archaeal genetic models allowing knockout and epitope tagging have led to significant increases in our understanding, including DNA polymerase roles in Okazaki fragment maturation on the lagging strand, towards reconstitution of the replisome itself. Furthermore, poorly characterised DNA polymerase paralogues are finding roles in DNA repair and CRISPR immunity. This review attempts to provide a current update on the roles of archaeal DNA polymerases in both DNA replication and repair, addressing significant questions that remain for this field.
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Yudkina, Anna V., Evgeniy S. Shilkin, Alena V. Makarova, and Dmitry O. Zharkov. "Stalling of Eukaryotic Translesion DNA Polymerases at DNA-Protein Cross-Links." Genes 13, no. 2 (January 18, 2022): 166. http://dx.doi.org/10.3390/genes13020166.

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DNA-protein cross-links (DPCs) are extremely bulky adducts that interfere with replication. In human cells, they are processed by SPRTN, a protease activated by DNA polymerases stuck at DPCs. We have recently proposed the mechanism of the interaction of DNA polymerases with DPCs, involving a clash of protein surfaces followed by the distortion of the cross-linked protein. Here, we used a model DPC, located in the single-stranded template, the template strand of double-stranded DNA, or the displaced strand, to study the eukaryotic translesion DNA polymerases ζ (POLζ), ι (POLι) and η (POLη). POLι demonstrated poor synthesis on the DPC-containing substrates. POLζ and POLη paused at sites dictated by the footprints of the polymerase and the cross-linked protein. Beyond that, POLζ was able to elongate the primer to the cross-link site when a DPC was in the template. Surprisingly, POLη was not only able to reach the cross-link site but also incorporated 1–2 nucleotides past it, which makes POLη the most efficient DNA polymerase on DPC-containing substrates. However, a DPC in the displaced strand was an insurmountable obstacle for all polymerases, which stalled several nucleotides before the cross-link site. Overall, the behavior of translesion polymerases agrees with the model of protein clash and distortion described above.
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Harada, Ryo, Yoshihisa Hirakawa, Akinori Yabuki, Yuichiro Kashiyama, Moe Maruyama, Ryo Onuma, Petr Soukal, et al. "Inventory and Evolution of Mitochondrion-localized Family A DNA Polymerases in Euglenozoa." Pathogens 9, no. 4 (April 1, 2020): 257. http://dx.doi.org/10.3390/pathogens9040257.

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The order Trypanosomatida has been well studied due to its pathogenicity and the unique biology of the mitochondrion. In Trypanosoma brucei, four DNA polymerases, namely PolIA, PolIB, PolIC, and PolID, related to bacterial DNA polymerase I (PolI), were shown to be localized in mitochondria experimentally. These mitochondrion-localized DNA polymerases are phylogenetically distinct from other family A DNA polymerases, such as bacterial PolI, DNA polymerase gamma (Polγ) in human and yeasts, “plant and protist organellar DNA polymerase (POP)” in diverse eukaryotes. However, the diversity of mitochondrion-localized DNA polymerases in Euglenozoa other than Trypanosomatida is poorly understood. In this study, we discovered putative mitochondrion-localized DNA polymerases in broad members of three major classes of Euglenozoa—Kinetoplastea, Diplonemea, and Euglenida—to explore the origin and evolution of trypanosomatid PolIA-D. We unveiled distinct inventories of mitochondrion-localized DNA polymerases in the three classes: (1) PolIA is ubiquitous across the three euglenozoan classes, (2) PolIB, C, and D are restricted in kinetoplastids, (3) new types of mitochondrion-localized DNA polymerases were identified in a prokinetoplastid and diplonemids, and (4) evolutionarily distinct types of POP were found in euglenids. We finally propose scenarios to explain the inventories of mitochondrion-localized DNA polymerases in Kinetoplastea, Diplonemea, and Euglenida.
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Hogg, Matthew, Pia Osterman, Göran Bylund, Rais Ganai, Else-Britt Lundström, Elisabeth Sauer-Eriksson, and Erik Johansson. "Structural basis for processive DNA synthesis by yeast DNA polymerase ε." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C200. http://dx.doi.org/10.1107/s205327331409799x.

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DNA polymerase ε (Pol ε) is a high-fidelity polymerase that participates in leading-strand synthesis during eukaryotic DNA replication in eukaryotic cells. The 2.2 Å ternary structure of the 142 kDa catalytic core of Pol ε from Saccharomyces cerevisiae in complex with DNA and an incoming nucleotide has recently been determined [1]. The structure provides information about the selection of the correct nucleotide and the positions of amino acids that might be critical for proofreading activity. Pol ε has the highest fidelity among B-family polymerases despite the absence of an extended β-hairpin loop that is required for high-fidelity replication by other B-family polymerases. Moreover, the catalytic core has a new domain (i.e. the P-domain) that allows Pol ε to encircle the nascent double-stranded DNA and enhance processifivity of the polymerase. The structure provides valuable insights into the similarities and differences between Pol ε and other B-family polymerases, and suggests possible mechanisms responsible for the high processivity and fidelity of Pol ε.
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Gibbs, J. S., K. Weisshart, P. Digard, A. deBruynKops, D. M. Knipe, and D. M. Coen. "Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site." Molecular and Cellular Biology 11, no. 9 (September 1991): 4786–95. http://dx.doi.org/10.1128/mcb.11.9.4786-4795.1991.

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Most DNA polymerases are multifunctional proteins that possess both polymerizing and exonucleolytic activities. For Escherichia coli DNA polymerase I and its relatives, polymerase and exonuclease activities reside on distinct, separable domains of the same polypeptide. The catalytic subunits of the alpha-like DNA polymerase family share regions of sequence homology with the 3'-5' exonuclease active site of DNA polymerase I; in certain alpha-like DNA polymerases, these regions of homology have been shown to be important for exonuclease activity. This finding has led to the hypothesis that alpha-like DNA polymerases also contain a distinct 3'-5' exonuclease domain. We have introduced conservative substitutions into a 3'-5' exonuclease active site homology in the gene encoding herpes simplex virus DNA polymerase, an alpha-like polymerase. Two mutants were severely impaired for viral DNA replication and polymerase activity. The mutants were not detectably affected in the ability of the polymerase to interact with its accessory protein, UL42, or to colocalize in infected cell nuclei with the major viral DNA-binding protein, ICP8, suggesting that the mutation did not exert global effects on protein folding. The results raise the possibility that there is a fundamental difference between alpha-like DNA polymerases and E. coli DNA polymerase I, with less distinction between 3'-5' exonuclease and polymerase functions in alpha-like DNA polymerases.
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Dissertations / Theses on the topic "DNA polymerases"

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Leavitt, Markley Carl. "Bacteriophage T5 DNA polymerase relationships of DNA polymerases." Diss., The University of Arizona, 1990. http://hdl.handle.net/10150/185335.

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T5 DNA polymerase, a highly processive single polypeptide enzyme, and PRD1 DNA polymerase, a protein-primed DNA polymerase, have been analyzed for their primary structural features. The amino acid sequence of T5 DNA polymerase reveals a high degree of homology with DNA polymerase I (Pol I) of Escherichia coli and retains many of the amino acid residues which have been implicated in the 3'-5' exonuclease and DNA polymerase activities of that enzyme. Alignment with sequences of polymerase I and T7 DNA polymerase (family A polymerases) was used to identify regions possibly involved in the high processivity of this enzyme. Further amino acid sequence comparisons of T5 DNA polymerase with a large group of DNA polymerases (family B) previously shown to exhibit little similarity to Pol I, indicate certain sequence segments are shared among distantly related DNA polymerases. These shared regions have been implicated in the 3'-5' exonuclease function of Pol I which suggests that the proofreading domains of all these enzymes may be related. Mutations in these segments in T5 DNA polymerase (family A) and PRD1 DNA polymerase (family B) greatly decrease the exonuclease activity of these enzymes but leave the polymerase activities intact. Additionally, an exonuclease deficient T5 DNA polymerase is used in DNA sequencing reactions and yields consistent results with low background contamination on autoradiographs of polyacrylamide/urea gels. PRD1 mutants defective in 3 regions which are highly conserved among family B DNA polymerases, are deficient in DNA polymerase activity but retain exonuclease activity.
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SALHI, SAMIA. "Dna polymerase de sulfolobus acidocaldarius : interet de l'etude des dna polymerases thermophiles." Paris 7, 1989. http://www.theses.fr/1989PA077169.

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La copie par la dna polymerase de sulfolobus acidocaldarius d'un dna simple brin uni-amorce de sequence connue a ete etudiee. Les parametres cinetiques affectant cette synthese dependent de la sequence du dna. La temperature de reaction a son importance. Les methodes employees sont la reaction polymerase en chaine, la mutagenese dirigee, le sequencage de sanger
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Pospiech, H. (Helmut). "The role of DNA polymerases, in particular DNA polymerase ε in DNA repair and replication." Doctoral thesis, University of Oulu, 2002. http://urn.fi/urn:isbn:9514266692.

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Abstract Analysis of the primary structure of DNA polymerase ε B subunit defined similarities to B subunits of eukaryotic DNA polymerases α, δ and ε as well as the small subunits of DNA polymerase DI of Euryarchaeota. Multiple sequence alignment of these proteins revealed the presence of 12 conserved motifs and defined a novel protein superfamily. The members of the B subunit family share a common domain architecture, suggesting a similar fold, and arguing for a conserved function among these proteins. The contribution of human DNA polymerase ε to nuclear DNA replication was studied using the antibody K18 that specifically inhibits the activity of this enzyme in vitro. This antibody significantly inhibited DNA synthesis both when microinjected into nuclei of exponentially growing human fibroblasts and in isolated HeLa cell nuclei, but did not inhibit SV40 DNA replication in vitro. These results suggest that the human DNA polymerase ε contributes substantially to the replicative synthesis of DNA and emphasises the differences between cellular replication and viral model systems. The human DNA polymerases ε and δ were found capable of gap-filling DNA synthesis during nucleotide excision repair in vitro. Both enzymes required PCNA and the clamp loader RFC, and in addition, polymerase δ required Fen-1 to prevent excessive displacement synthesis. Nucleotide excision repair of a defined DNA lesion was completely reconstituted utilising largely recombinant proteins, only ligase I and DNA polymerases δ and ε provided as highly purified human enzymes. This system was also utilised to study the role of the transcription factor II H during repair. Human non-homologous end joining of model substrates with different DNA end configurations was studied in HeLa cell extracts. This process depended partially on DNA synthesis as an aphidicolin-dependent DNA polymerase was required for the formation of a subset of end joining products. Experiments with neutralising antibodies reveal that DNA polymerase α but not DNA polymerases β or ε, may represent this DNA polymerase activity. Our results indicate that DNA synthesis contributes to the stability of DNA ends, and influences both the efficiency and outcome of the end joining event. Furthermore, our results suggest a minor role of PCNA in non-homologous end joining.
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Roettger, Michelle P. "Insight into the Fidelity of Two X-Family Polymerases: DNA Polymerase Mu and DNA Polymerase Beta." Columbus, Ohio : Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1211074588.

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Brown, Jessica Ann. "Kinetic Mechanisms of DNA Polymerases." The Ohio State University, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=osu1290014566.

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Morant, Nick. "Novel thermostable DNA polymerases for isothermal DNA amplification." Thesis, University of Bath, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.667735.

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DNA polymerases play a fundamental role in the transmission and maintenance of genetic information and have become an important in vitro diagnostic and analytical tool. The Loop-mediated isothermal DNA amplification (LAMP) method has major applications for disease and pathogen detection and utilises the unique strand-displacement activity of a small group of thermostable DNA polymerases. The Large (Klenow-like) Fragment of Geobacillus stearothermophilus DNA polymerase I (B.st LF Pol I) currently serves as the enzyme of choice for the majority of these isothermal reactions, with few alternatives commercially available. An increasing need for point-of-care nucleic acid diagnostics is now shifting detection methods away from traditional laboratory based chemistries, such as the polymerase chain reaction (PCR), in favour of faster, and often simpler, isothermal methods. It was recognised that in order to facilitate these rapid isothermal reactions there was a requirement for alternative thermostable, strand-displacing DNA polymerases and this was the basis of this thesis. This thesis reports the successful identification of polymerases from Family A, chosen for their inherent strand-displacement activity, which is essential for the removal of RNA primers of Okazaki fragments during lagging-strand DNA synthesis in vivo. Twelve thermophilic organisms, with growth temperature ranges between 50oC and 80oC, were identified and the genomic DNA extracted. Where DNA sequences were unavailable, a gene-walking technique revealed the polA sequences, enabling the Large Fragment Pol I to be cloned and the recombinant protein over-expressed in Escherichia coli. A three-stage column chromatography purification permitted the characterisation of ten newly identified Pol I enzymes suitable for use in LAMP. Thermodesulfatator indicus (T.in) Pol I proved to be the most interesting enzyme isolated. Demonstrating strong strand-displacement activity and thermostability to 98oC, T.in Pol I is uniquely suitable to a newly termed heat-denaturing LAMP (HD-LAMP) reaction offering many potential advantages over the existing LAMP protocol. The current understanding of strand-displacement activity of Pol I is poorly understood. This thesis recognised the need to identify the exact regions and motifs responsible for this activity of the enzyme, enabling potential enhancements to be made. Enzyme engineering using site-directed mutagenesis and the formation of chimeras confirmed the importance of specific subdomains in strand-separation activity. With this knowledge, a unique Thermus aquaticus (T.aq) Pol I mutant demonstrated sufficient strand-displacement activity to permit its use in LAMP for the first time. The fusion of Cren7, a double-stranded DNA binding protein, to Pol I for use in LAMP is also reported. Although the fusion construct was found to reduce amplification speed, enhancements were observed in the presence of increased salt concentrations and it is suggested here as a means for future enzyme development.
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Elshawadfy, Ashraf Mohamed. "Engineering archaeal DNA polymerases for biotechnology applications." Thesis, University of Newcastle Upon Tyne, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.606814.

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The DNA polymerase from the archaeon Pyrococcus furiosus (Pfu- Pol) is commonly used in the polymerase chain reaction (PCR). The enzyme has high thermostability and is very accurate due to the presence of 3'---5'exonuclease (proofreading) activity. Unfortunately, the polymerase has relatively low processivity, limiting its ability to amplify long stretches of DNA relatively quickly. In this project, two approaches have been used in an attempt to improve the performance and processivity of Pfu DNA polymerase in PCR applications. In the first, the overall positive charge of the protein has been increased; predicted to increase electrostatic interactions between the negatively charged DNA and the more positively charged proteins. In the second, we have prepared a set of Pfu-Pol mutants in an attempt to make Pfu-Pol more similar to KODl; a polymerase isolated from a related hyperthermophilic archaeon Thermocococcus kodakaraensis. KODl is known to have a higher processivity than Pfu-Pol and both share a 3'---5' proof reading exonuclease activity. A PCR-based protocol was used to introduce the desired mutations.
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Wardle, Josephine. "Recognition of deaminated bases by DNA polymerases." Thesis, University of Newcastle Upon Tyne, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.443025.

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MENTEGARI, ELISA. "DNA damage tolerance by specialized DNA polymerases in humans and plants." Doctoral thesis, Università degli studi di Pavia, 2018. http://hdl.handle.net/11571/1243288.

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Plaskon, Randolph Richard. "DNA curvature and fluctuational base pair opening in the promoter regions of escherichia coli." Diss., Georgia Institute of Technology, 1988. http://hdl.handle.net/1853/25323.

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Books on the topic "DNA polymerases"

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Hübscher, Ulrich. DNA polymerases: Discovery, characterization, and functions in cellular DNA transactions. New Jersey: World Scientific, 2010.

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A, Loeb Lawrence, ed. Animal cell DNA polymerases. Boca Raton, Fla: CRC Press, 1986.

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1943-, Erlich Henry A., ed. PCR technology: Principles and applications for DNA amplification. New York: Stockton Press, 1989.

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1943-, Erlich Henry A., ed. PCR technology: Principles and applications for DNA amplification. Houndmills, Busingstoke, Hants, England: Macmillan Publishers, 1989.

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L, Campbell Judith, ed. DNA replication. San Diego, Calif: Academic, 1995.

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Cullmann, Gerhard. Klonierung und Charakterisierung der Maus DNA-Polymerase [delta]. Konstanz: Hartung-Gorre, 1993.

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Carstens, Russ P. Identification of RNA splicing errors resulting in human ornithine transcarbamylase deficiency. [New Haven: s.n.], 1990.

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Travers, A. A. DNA-protein interactions. London: Chapman & Hall, 1993.

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P, Hollenberg C., and Sahm H, eds. Therapeutics, diagnostics, cell cultures, and product isolation. Stuttgart: Gustav Fischer, 1990.

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Artsimovitch, Irina, and Thomas J. Santangelo. Bacterial transcriptional control: Methods and protocols. New York: Humana Press, 2015.

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Book chapters on the topic "DNA polymerases"

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Lygerou, Zoi. "DNA Polymerases." In Encyclopedia of Systems Biology, 610. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_1442.

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Sobol, Robert W. "DNA Repair Polymerases." In Nucleic Acid Polymerases, 43–83. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-39796-7_3.

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Laos, Roberto, Ryan W. Shaw, and Steven A. Benner. "Engineered DNA Polymerases." In Nucleic Acid Polymerases, 163–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-39796-7_7.

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Berdis, Anthony J. "DNA Polymerases That Perform Template-Independent DNA Synthesis." In Nucleic Acid Polymerases, 109–37. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-39796-7_5.

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Walsh, Erin, and Kristin A. Eckert. "Eukaryotic Replicative DNA Polymerases." In Nucleic Acid Polymerases, 17–41. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-39796-7_2.

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Choi, Jeong-Yun, Robert L. Eoff, and F. Peter Guengerich. "Bypass DNA Polymerases." In Chemical Carcinogenesis, 345–73. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-61737-995-6_16.

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McGregor, W. Glenn. "Translesion DNA Polymerases." In Encyclopedia of Cancer, 1–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_5938-2.

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Villani, Giuseppe, and Nicolas Tanguy Le Gac. "DNA Repair Polymerases." In Molecular Life Sciences, 1–13. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-6436-5_61-1.

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McGregor, W. Glenn. "Translesion DNA Polymerases." In Encyclopedia of Cancer, 4641–43. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_5938.

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Villani, Giuseppe, and Nicolas Tanguy Le Gac. "DNA Repair Polymerases." In Molecular Life Sciences, 240–51. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4614-1531-2_61.

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Conference papers on the topic "DNA polymerases"

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"Noncanonical prokaryotic X family DNA polymerases." In Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-088.

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Obeid, Samra, Nina Blatter, and Andreas Marx. "Lost in replication: DNA polymerases encountering non-instructive DNA lesions." In XVth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2011. http://dx.doi.org/10.1135/css201112027.

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Bergen, Konrad, Holger Busskamp, Anna-Lena Steck, Samra Obeid, Karin Betz, and Andreas Marx. "DNA polymerases in action with modified substrates." In XVIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2014. http://dx.doi.org/10.1135/css201414101.

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Kielkowski, Pavel, and Michal Hocek. "Competitive incorporations of modified versus natural nucleotides by DNA polymerases." In XVIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2014. http://dx.doi.org/10.1135/css201414295.

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Singatulina, A. S., M. V. Sukhanova, and O. I. Lavrik. "FACTOR HPF1 REGULATES THE ACTIVITY OF POLY(ADP-RIBOSE)POLYMERASES 1 AND 2 AND THE FORMATION OF POLY(ADP-RIBOSE)-CONTAINING COMPARTMENTS WITH THE PARTICIPATION OF THE RNA-BINDING PROTEIN FUS." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-281.

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Poly(ADP-ribose) polymerases 1 and 2 (PARP1/2) synthesize poly(ADP-ribose) (PAR) by covalently modifying a number of proteins involved in DNA/RNA metabolism, including themselves. PARP1/2 are key regulators of DNA repair via autopoly(ADP-ribosyl)ation at the site of DNA damage. The study of factors that modulate PARP1/2 activity in response to genotoxic stress is an important task in modern biology.
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Cavanaugh, Nisha, Michael Trostler, Jennifer Patro, Jeff Beckman, and Robert D. Kuchta. "Mechanisms by which DNA polymerases discriminate between right and wrong dNTPs." In XIVth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2008. http://dx.doi.org/10.1135/css200810186.

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Latancia, Marcela Teatin, André Uchimura Bastos, Natália Cestari Moreno, Davi Jardim, Clarissa RR Rocha, and Carlos FM Menck. "Abstract 4089: Investigating translesion synthesis DNA polymerases roles on tumor protection after temozolomide induced DNA damage." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-4089.

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Birkuš, Gabriel, Ivan Votruba, Antonín Holý, and Berta Otová. "HPMPApp as a substrate toward replicative DNA polymerases α, δ and ε." In XIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199902289.

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Lee, Tae Yoon, Dimistris E. Nikitopoulos, Daniel S. Park, Steven A. Soper, and Michael C. Murphy. "Design and Fabrication of a Ligase Detection Reaction (LDR) Microchip With an Integrated Passive Micromixer." In ASME 2007 International Mechanical Engineering Congress and Exposition. ASMEDC, 2007. http://dx.doi.org/10.1115/imece2007-42216.

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The ligase detection reaction (LDR) is a technique that can distinguish low-abundant mutant DNAs from wild-type DNAs. LDR is usually carried out on DNAs amplified using the polymerase chain reaction (PCR). In the realization of modular microfluidic systems, the DNA output of the PCR handed off to the LDR chip needs to be mixed with LDR reagents before continuing the reaction. Polymer, continuous flow ligase detection reaction (CFLDR) devices with integrated passive micromixers, were designed, fabricated and tested. The devices each consisted of: a passive mixer for mixing a PCR sample, a cocktail of primers, and ligase, an enzyme of DNA; an incubator channel (95°C) for preheating the mixture; and a thermal cycling channel for the LDR. The devices were produced by hot embossing polycarbonate (PC) substrates with brass mold inserts manufactured by micro-milling. Experiments using food dyes showed that the appropriate mixture concentrations were delivered to the preheating channel in both the pulling and pushing modes.
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Persat, Alexandre, Tomoyuki Morita, and Juan G. Santiago. "On-Chip Isothermal Polymerase Chain Reaction." In ASME 2007 International Mechanical Engineering Congress and Exposition. ASMEDC, 2007. http://dx.doi.org/10.1115/imece2007-43070.

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We present a novel technique for on-chip PCR where temperature is held constant and uniform in the reactor. Specific chemicals, known as denaturants, have the ability to melt DNA. A flow control scheme establishes spatio-temporal fluctuations in the concentration of denaturants along a microchannel, while electromigration drives DNA through this spatially varying denaturant concentration field. Preliminary results show denaturation and extension of a 200 base pairs (bp) DNA template.
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Reports on the topic "DNA polymerases"

1

Kuchta, Robert D. Fidelity Mechanisms of DNA Polymerase Alpha. Fort Belvoir, VA: Defense Technical Information Center, July 2008. http://dx.doi.org/10.21236/ada499543.

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Hecht, Sidney M. Inhibition of Malarial DNA Polymerase Alpha. Fort Belvoir, VA: Defense Technical Information Center, November 1990. http://dx.doi.org/10.21236/adb151470.

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Mishra, N. C. Characterization of the mammalian DNA polymerase gene and protein. Annual progress report. Office of Scientific and Technical Information (OSTI), January 1993. http://dx.doi.org/10.2172/90178.

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Mishra, N. C. Characterization of the mammalian DNA polymerase gene and protein. Annual progress report. Office of Scientific and Technical Information (OSTI), January 1992. http://dx.doi.org/10.2172/10165626.

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Makridakis, Nick. Variations of Human DNA Polymerase Genes as Biomarkers of Prostate Cancer Progression. Fort Belvoir, VA: Defense Technical Information Center, July 2013. http://dx.doi.org/10.21236/ada591964.

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Lee, Marietta. Role of Human DNA Polymerase and Its Accessory Proteins in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 1998. http://dx.doi.org/10.21236/ada382695.

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Makridakis, Nick. Variations of Human DNA Polymerase Genes as Biomarkers of Prostate Cancer Progression. Fort Belvoir, VA: Defense Technical Information Center, July 2011. http://dx.doi.org/10.21236/ada548987.

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Mishra, N. C. Characterization of the mammalian DNA polymerase gene(s) and enzyme(s). Annual progress report. Office of Scientific and Technical Information (OSTI), January 1995. http://dx.doi.org/10.2172/89557.

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Mishra, N. C. Characterization of the mammalian DNA polymerase gene(s) and enzyme(s). Annual progress report. Office of Scientific and Technical Information (OSTI), January 1994. http://dx.doi.org/10.2172/89558.

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Laurence, Jeffrey. Antibody to the RNA-Dependent DNA Polymerase of HTLV-III: Characterization and Clinical Associations. Fort Belvoir, VA: Defense Technical Information Center, March 1990. http://dx.doi.org/10.21236/ada231466.

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