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The proofreading activity of DNA polymerase delta (show POLD1 Proteins) plays a role in shunting DNA mismatch repair to an EXO1 (show EXO1 Proteins)-dependent excision pathway as opposed to directly participating in gap formation via its 3'-5' exonuclease (show EXOSC10 Proteins) activity.
The mitotic DNA synthesis is RAD52 (show RAD52 Proteins) dependent, and RAD52 (show RAD52 Proteins) is required for the timely recruitment of MUS81 (show MUS81 Proteins) and POLD3 to common fragile sites in early mitosis.
Studies indicate that DNA polymerase delta 3 (Pol delta3) exhibits significant differences in properties with a major impact on cellular processes in genomic surveillance, DNA replication and DNA repair.
Data suggest that relatively high affinity binding of PolD3-RIR (show APBB1 Proteins) motif to Rev1 (show REV1 Proteins)-C-terminal domain displaces subunits from PolN, Pol-iota (show POLM Proteins), or PolK (show PAPD7 Proteins) from Rev1 (show REV1 Proteins) complex and promotes formation of Rev1 (show REV1 Proteins)/PolZ4 assembly with PCNA (show PCNA Proteins) for translesion DNA replication.
POLD3 is SUMOylated by SUMO2 (show SUMO2 Proteins) in response to replication stress and could play an important role in the regulation of cellular response to DNA replication stress.
Findings provide evidence for the novel concept that Pol delta3 has a role in lagging strand synthesis, and that both forms of Pol delta3 and 4 may participate in DNA replication in higher eukaryotic cells.
In a cyclin E (show CCNE1 Proteins) overexpression model of DNA replication stress, POLD3, the human ortholog of POL32, was required for cell cycle progression and processive DNA synthesis.
Pol delta3 is the predominant form of Pol delta (show POLD1 Proteins) at sites of UV damage as a result of p12 (show POLE4 Proteins) degradation; results show that Pol delta (show POLD1 Proteins) at the DNA damage site is the Pol delta (show POLD1 Proteins) trimer lacking p12 (show POLE4 Proteins) regardless of the cell cycle phase
We identified three new CRC risk loci at 6p21 (rs1321311, near CDKN1A; P = 1.14 x 10(-10)), 11q13.4 (rs3824999, intronic to POLD3; P = 3.65 x 10(-10)) and Xp22.2 (rs5934683, near SHROOM2; P = 7.30 x 10(-10)).
Serine-458, located in the proliferating cell nuclear antigen (PCNA (show PCNA Proteins))-interacting motif of Poldelta(p68 (show ANXA6 Proteins)), is a phosphorylation site for protein kinase A (PKA); p68 (show ANXA6 Proteins) mutation results in decreased p68 (show ANXA6 Proteins) affinity for PCNA (show PCNA Proteins) as well as processivity of Poldelta.
POLD3 deficiency is lethal in mice, Pold3 heterozygous mice are born at sub-Mendelian ratios.
This gene encodes the 66-kDa subunit of DNA polymerase delta. DNA polymerase delta possesses both polymerase and 3' to 5' exonuclease activity and plays a critical role in DNA replication and repair. The encoded protein plays a role in regulating the activity of DNA polymerase delta through interactions with other subunits and the processivity cofactor proliferating cell nuclear antigen (PCNA). Alternatively spliced transcript variants have been observed for this gene.
DNA-directed DNA polymerase delta 3
, DNA polymerase delta p66 subunit
, DNA polymerase delta subunit 3
, polymerase (DNA-directed), delta 3, accessory subunit
, DNA polymerase delta subunit 3-like
, DNA polymerase delta subunit p66
, Pol delta C subunit (p66)
, polymerase (DNA directed), delta 3