Academic literature on the topic 'DNA polymerases ; DNA replication ; Cell division'

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Journal articles on the topic "DNA polymerases ; DNA replication ; Cell division"

1

Burke, Cassandra R., and Andrej Lupták. "DNA synthesis from diphosphate substrates by DNA polymerases." Proceedings of the National Academy of Sciences 115, no. 5 (2018): 980–85. http://dx.doi.org/10.1073/pnas.1712193115.

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The activity of DNA polymerase underlies numerous biotechnologies, cell division, and therapeutics, yet the enzyme remains incompletely understood. We demonstrate that both thermostable and mesophilic DNA polymerases readily utilize deoxyribonucleoside diphosphates (dNDPs) for DNA synthesis and inorganic phosphate for the reverse reaction, that is, phosphorolysis of DNA. For Taq DNA polymerase, the KMs of the dNDP and phosphate substrates are ∼20 and 200 times higher than for dNTP and pyrophosphate, respectively. DNA synthesis from dNDPs is about 17 times slower than from dNTPs, and DNA phosph
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2

Leal, Andrea Zurita, Marie Schwebs, Emma Briggs, et al. "Genome maintenance functions of a putative Trypanosoma brucei translesion DNA polymerase include telomere association and a role in antigenic variation." Nucleic Acids Research 48, no. 17 (2020): 9660–80. http://dx.doi.org/10.1093/nar/gkaa686.

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Abstract Maintenance of genome integrity is critical to guarantee transfer of an intact genome from parent to offspring during cell division. DNA polymerases (Pols) provide roles in both replication of the genome and the repair of a wide range of lesions. Amongst replicative DNA Pols, translesion DNA Pols play a particular role: replication to bypass DNA damage. All cells express a range of translesion Pols, but little work has examined their function in parasites, including whether the enzymes might contribute to host-parasite interactions. Here, we describe a dual function of one putative tr
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3

McGlynn, Peter. "Helicases that underpin replication of protein-bound DNA in Escherichia coli." Biochemical Society Transactions 39, no. 2 (2011): 606–10. http://dx.doi.org/10.1042/bst0390606.

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A pre-requisite for successful cell division in any organism is synthesis of an accurate copy of the genetic information needed for survival. This copying process is a mammoth task, given the amount of DNA that must be duplicated, but potential blocks to replication fork movement also pose a challenge for genome duplication. Damage to the template inhibits the replication machinery but proteins bound to the template such as RNA polymerases also present barriers to replication. This review discusses recent results from Escherichia coli that shed light on the roles of helicases in overcoming pro
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4

Pollok, S., J. Stoepel, C. Bauerschmidt, E. Kremmer, and H. P. Nasheuer. "Regulation of eukaryotic DNA replication at the initiation step." Biochemical Society Transactions 31, no. 1 (2003): 266–69. http://dx.doi.org/10.1042/bst0310266.

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The studies of cell growth and division have remained at the centre of biomedical research for more than 100 years. The combination of genetic, biochemical, molecular and cell biological techniques recently yielded a burst in what is known of the molecular control of cell growth processes. The initiation of DNA replication is crucial for the stability of the genetic information of a cell. Two factors, Cdc45p (cell division cycle 45p) and DNA polymerase α-primase, are necessary in this process. Depending on growth signals, Cdc45p is expressed as a late protein. New phosphorylation-specific anti
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5

Corellou, F., S. R. Bisgrove, D. L. Kropf, L. Meijer, B. Kloareg, and F. Y. Bouget. "A S/M DNA replication checkpoint prevents nuclear and cytoplasmic events of cell division including centrosomal axis alignment and inhibits activation of cyclin-dependent kinase-like proteins in fucoid zygotes." Development 127, no. 8 (2000): 1651–60. http://dx.doi.org/10.1242/dev.127.8.1651.

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S/M checkpoints prevent various aspects of cell division when DNA has not been replicated. Such checkpoints are stringent in yeast and animal somatic cells but are usually partial or not present in animal embryos. Because little is known about S/M checkpoints in plant cells and embryos, we have investigated the effect of aphidicolin, a specific inhibitor of DNA polymerases (alpha) and (delta), on cell division and morphogenesis in Fucus and Pelvetia zygotes. Both DNA replication and cell division were inhibited by aphidicolin, indicating the presence, in fucoid zygotes, of a S/M checkpoint. Th
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6

Smith, Roger K. W., and Martin H. Johnson. "DNA replication and compaction in the cleaving embryo of the mouse." Development 89, no. 1 (1985): 133–48. http://dx.doi.org/10.1242/dev.89.1.133.

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The effects of aphidicolin, a reversible inhibitor of DNA polymerase alpha, both on replication and on development of the mouse embryo from the 2- and 4-cell stages to the compacted late 8-cell stage have been assessed. The continuous presence of aphidicolin from G1 of the 4-cell stage resulted in inhibition of DNA replication and prevention of division from 4 to 8 cells, but was without effect on the timing or incidence of cell flattening, surface polarization and cytoplasmic polarization. The continuous presence of aphidicolin from G1 of the 2-cell stage resulted in inhibition of DNA replica
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7

Mass, Gilad, Tamar Nethanel, and Gabriel Kaufmann. "The Middle Subunit of Replication Protein A Contacts Growing RNA-DNA Primers in Replicating Simian Virus 40 Chromosomes." Molecular and Cellular Biology 18, no. 11 (1998): 6399–407. http://dx.doi.org/10.1128/mcb.18.11.6399.

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ABSTRACT The eukaryotic single-stranded DNA binding protein replication protein A (RPA) participates in major DNA transactions. RPA also interacts through its middle subunit (Rpa2) with regulators of the cell division cycle and of the response to DNA damage. A specific contact between Rpa2 and nascent simian virus 40 DNA was revealed by in situ UV cross-linking. The dynamic attributes of the cross-linked DNA, namely, its size distribution, RNA primer content, and replication fork polarity, were determined. These data suggest that Rpa2 contacts the early DNA chain intermediates synthesized by D
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8

Yang, Hui, Daoquan Xiang, Sathya Prakash Venglat, et al. "PolA2 is required for embryo development in ArabidopsisThis paper is one of a selection of papers published in a Special Issue from the National Research Council of Canada – Plant Biotechnology Institute." Botany 87, no. 6 (2009): 626–34. http://dx.doi.org/10.1139/b09-028.

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DNA replication machinery is highly conserved in eukaryotes. DNA polymerase is essential for the synthesis of new DNA strands and for DNA repair. Despite the significant progress in the understanding of these processes in yeast and animal model systems, there is only scant information available for their counterparts in plants. Among different multisubunit-containing DNA polymerases, DNA polymerase α (POLA complex) is composed of four subunits. In this study, we report on the characterization of PolA2, which encodes the putative B subunit of DNA polymerase α in Arabidopsis thaliana (L.) Heynh.
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9

Holway, Antonia H., Seung-Hwan Kim, Adriana La Volpe, and W. Matthew Michael. "Checkpoint silencing during the DNA damage response in Caenorhabditis elegans embryos." Journal of Cell Biology 172, no. 7 (2006): 999–1008. http://dx.doi.org/10.1083/jcb.200512136.

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In most cells, the DNA damage checkpoint delays cell division when replication is stalled by DNA damage. In early Caenorhabditis elegans embryos, however, the checkpoint responds to developmental signals that control the timing of cell division, and checkpoint activation by nondevelopmental inputs disrupts cell cycle timing and causes embryonic lethality. Given this sensitivity to inappropriate checkpoint activation, we were interested in how embryos respond to DNA damage. We demonstrate that the checkpoint response to DNA damage is actively silenced in embryos but not in the germ line. Silenc
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10

Hazeslip, Lindsey, Maroof Khan Zafar, Muhammad Zain Chauhan, and Alicia K. Byrd. "Genome Maintenance by DNA Helicase B." Genes 11, no. 5 (2020): 578. http://dx.doi.org/10.3390/genes11050578.

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DNA Helicase B (HELB) is a conserved helicase in higher eukaryotes with roles in the initiation of DNA replication and in the DNA damage and replication stress responses. HELB is a predominately nuclear protein in G1 phase where it is involved in initiation of DNA replication through interactions with DNA topoisomerase 2-binding protein 1 (TOPBP1), cell division control protein 45 (CDC45), and DNA polymerase α-primase. HELB also inhibits homologous recombination by reducing long-range end resection. After phosphorylation by cyclin-dependent kinase 2 (CDK2) at the G1 to S transition, HELB is pr
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