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- W1008279511 abstract "PrimPol is a recently identified member of the archaeo-eukaryotic primase (AEP) familyof proteins. It possesses both primase and polymerase activities and is involved in thereplication of both nuclear and mitochondrial DNA. PrimPol is predicted to possess anAEP polymerase and a UL52-like zinc finger domain. This thesis establishes the rolesof these domains in the context of PrimPol’s catalytic activities. Although apparentlydispensable for polymerase activity, the zinc finger is essential for maintaining primaseactivity and also appears to play an important role in regulating the processivity andfidelity of PrimPol’s extension activities. A recently study identified a PrimPol mutation(Y89D) that is potentially associated with the development of high myopia in humans.Here, the biochemical defects associated with this mutant are analysed and described.This protein variant has a significant reduction in polymerase activity. Mutationalanalysis suggests that the hydrophobic ring of tyrosine is important for retaining wildtypeDNA extension activity. Biophysical analysis of the secondary structure andstability of this PrimPol variant suggests that this PrimPol variant has reduced α-helicalcontent and is less stable than the wild-type protein.Finally, the interaction of PrimPol with single-stranded DNA binding protein replicationprotein A (RPA) is investigated. Previous studies have identified an interaction ofPrimPol with RPA. Here, it is demonstrated that PrimPol has two separate RPAinteraction motifs and a crystal structure is presented of one such motif in PrimPolbound to RPA that reveals the molecular basis for this interaction.Together, these studies provide molecular insights into the catalytic mechanism ofPrimPol as well as some of the key intramolecular and intermolecular mechanisms ofthat regulate the activities of PrimPol." @default.
- W1008279511 created "2016-06-24" @default.
- W1008279511 creator A5000679200 @default.
- W1008279511 date "2015-05-18" @default.
- W1008279511 modified "2023-09-27" @default.
- W1008279511 title "Molecular dissection of PrimPol, a novel primase-polymerase involved in damage tolerance during DNA replication in eukaryotic cells" @default.
- W1008279511 hasPublicationYear "2015" @default.
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