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dc.contributor.authorZaher, Manal S.
dc.contributor.authorOke, Muse
dc.contributor.authorHamdan, Samir
dc.date.accessioned2017-04-13T11:50:56Z
dc.date.available2017-04-13T11:50:56Z
dc.date.issued2014-11-21
dc.identifier.citationZaher MS, Oke M, Hamdan SM (2014) Eukaryotic DNA Replicases. Molecular Life Sciences: 1–22. Available: http://dx.doi.org/10.1007/978-1-4614-6436-5_55-4.
dc.identifier.doi10.1007/978-1-4614-6436-5_55-4
dc.identifier.doi10.1007/978-1-4614-1531-2_55
dc.identifier.urihttp://hdl.handle.net/10754/623133
dc.description.abstractThe current model of the eukaryotic DNA replication fork includes three replicative DNA polymerases, polymerase α/primase complex (Pol α), polymerase δ (Pol δ), and polymerase ε (Pol ε). The primase synthesizes 8–12 nucleotide RNA primers that are extended by the DNA polymerization activity of Pol α into 30–35 nucleotide RNA-DNA primers. Replication factor C (RFC) opens the polymerase clamp-like processivity factor, proliferating cell nuclear antigen (PCNA), and loads it onto the primer-template. Pol δ utilizes PCNA to mediate highly processive DNA synthesis, while Pol ε has intrinsic high processivity that is modestly stimulated by PCNA. Pol ε replicates the leading strand and Pol δ replicates the lagging strand in a division of labor that is not strict. The three polymerases are comprised of multiple subunits and share unifying features in their large catalytic and B subunits. The remaining subunits are evolutionarily not related and perform diverse functions. The catalytic subunits are members of family B, which are distinguished by their larger sizes due to inserts in their N- and C-terminal regions. The sizes of these inserts vary among the three polymerases, and their functions remain largely unknown. Strikingly, the quaternary structures of Pol α, Pol δ, and Pol ε are arranged similarly. The catalytic subunits adopt a globular structure that is linked via its conserved C-terminal region to the B subunit. The remaining subunits are linked to the catalytic and B subunits in a highly flexible manner.
dc.publisherSpringer Nature
dc.relation.urlhttp://link.springer.com/chapter/10.1007/978-1-4614-6436-5_55-4
dc.titleEukaryotic DNA Replicases
dc.typeBook Chapter
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentLaboratory of DNA Replication and Recombination
dc.identifier.journalMolecular Life Sciences
kaust.personZaher, Manal S.
kaust.personOke, Muse
kaust.personHamdan, Samir


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