scholarly journals PDIP46 (DNA polymerase δ interacting protein 46) is an activating factor for human DNA polymerase δ

Oncotarget ◽  
2016 ◽  
Vol 7 (5) ◽  
pp. 6294-6313 ◽  
Author(s):  
Xiaoxiao Wang ◽  
Sufang Zhang ◽  
Rong Zheng ◽  
Fu Yue ◽  
Szu Hua Sharon Lin ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Interacting Protein ◽  
Dna Polymerase Δ ◽  
Human Dna

scholarly journals Identification of PCNA-interacting protein motifs in human DNA polymerase δ

2020 ◽  
Vol 40 (4) ◽  
Author(s):  
Prashant Khandagale ◽  
Shweta Thakur ◽  
Narottam Acharya
Keyword(s):  
Dna Polymerase ◽  
Proliferating Cell Nuclear Antigen ◽  
Nuclear Antigen ◽  
Protein Motif ◽  
Interacting Protein ◽  
Protein Motifs ◽  
Dna Polymerase Δ ◽  
Human Dna ◽  
Processivity Factor ◽  
Proliferating Cell

Abstract DNA polymerase δ (Polδ) is a highly processive essential replicative DNA polymerase. In humans, the Polδ holoenzyme consists of p125, p50, p68 and p12 subunits and recently, we showed that the p12 subunit exists as a dimer. Extensive biochemical studies suggest that all the subunits of Polδ interact with the processivity factor proliferating cell nuclear antigen (PCNA) to carry out a pivotal role in genomic DNA replication. While PCNA-interacting protein motif (PIP) motifs in p68, p50 and p12 have been mapped, same in p125, the catalytic subunit of the holoenzyme, remains elusive. Therefore, in the present study by using multiple approaches we have conclusively mapped a non-canonical PIP motif from residues 999VGGLLAFA1008 in p125, which binds to the inter-domain-connecting loop (IDCL) of PCNA with high affinity. Collectively, including previous studies, we conclude that similar to Saccharomyces cerevisiae Polδ, each of the human Polδ subunits possesses motif to interact with PCNA and significantly contributes toward the processive nature of this replicative DNA polymerase.

scholarly journals Functional Roles of p12, the Fourth Subunit of Human DNA Polymerase δ

2006 ◽  
Vol 281 (21) ◽  
pp. 14748-14755 ◽  
Author(s):  
Hao Li ◽  
Bin Xie ◽  
Yajing Zhou ◽  
Amal Rahmeh ◽  
Sandra Trusa ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Functional Roles ◽  
Dna Polymerase Δ ◽  
Human Dna

scholarly journals Proofreading exonuclease activity of human DNA polymerase δ and its effects on lesion-bypass DNA synthesis

2009 ◽  
Vol 37 (9) ◽  
pp. 2854-2866 ◽  
Author(s):  
Ruzaliya Fazlieva ◽  
Cynthia S. Spittle ◽  
Darlene Morrissey ◽  
Harutoshi Hayashi ◽  
Hong Yan ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Exonuclease Activity ◽  
Lesion Bypass ◽  
Dna Polymerase Δ ◽  
Human Dna

scholarly journals Further Characterization of Human DNA Polymerase δ Interacting Protein 38

2005 ◽  
Vol 280 (23) ◽  
pp. 22375-22384 ◽  
Author(s):  
Bin Xie ◽  
Hao Li ◽  
Qi Wang ◽  
Suqing Xie ◽  
Amal Rahmeh ◽  
...  
Keyword(s):  
Dna Repair ◽  
Amino Acid ◽  
Dna Replication ◽  
Dna Polymerase ◽  
Mitochondrial Protein ◽  
Nuclear Antigen ◽  
Amino Acid Residues ◽  
Mitochondrial Targeting ◽  
Interacting Protein ◽  
Human Dna

Polymerase δ interacting protein 38 (PDIP38) was identified as a human DNA polymerase (pol) δ interacting protein through a direct interaction with p50, the small subunit of human pol δ. PDIP38 was also found to interact with proliferating cell nuclear antigen, which suggested that it might play a role in vivo in the processes of DNA replication and DNA repair in the nucleus. In order to characterize further this novel protein, we have examined its subcellular localization by the use of immunochemical and cellular fractionation techniques. These studies show that PDIP38 is a novel mitochondrial protein and is localized mainly to the mitochondria. PDIP38 was shown to possess a functional mitochondrial targeting sequence that is located within the first 35 N-terminal amino acid residues. The mature PDIP38 protein is about 50 amino acid residues smaller than the full-length precursor PDIP38 protein, consistent with it being processed by cleavage of the mitochondrial targeting sequence during entry into the mitochondria. His-tagged mature PDIP38 inhibited pol δ activity in vitro and interacted with human papillomavirus 16 E7 oncoprotein, suggesting that PDIP38 might play a role in the pol δ-mediated viral DNA replication. Although the localization of PDIP38 to the mitochondria suggests that it serves functions within the mitochondria, we cannot eliminate the possibility that it may be involved in pol δ-mediated DNA replication or DNA repair under certain conditions such as viral infection.

Human DNA polymerase δ gene maps to region 19q13.3–q13.4 by in Situ hybridization

Genomics ◽  
1992 ◽  
Vol 14 (1) ◽  
pp. 205-206 ◽  
Author(s):  
Robert R. Kemper ◽  
Eugene R. Ahn ◽  
Peng Zhang ◽  
Marietta Y.W.T. Lee ◽  
Mark Rabin
Keyword(s):  
In Situ Hybridization ◽  
Dna Polymerase ◽  
Dna Polymerase Δ ◽  
Human Dna ◽  
Gene Maps

Structure of the Gene for the Catalytic Subunit of Human DNA Polymerase δ (POLD1)

Genomics ◽  
1995 ◽  
Vol 28 (3) ◽  
pp. 411-419 ◽  
Author(s):  
Long-Sheng Chang ◽  
Lingyun Zhao ◽  
Lingyun Zhu ◽  
Meei-Ling Chen ◽  
Marietta Y.W.T. Lee
Keyword(s):  
Dna Polymerase ◽  
Catalytic Subunit ◽  
Dna Polymerase Δ ◽  
Human Dna

scholarly journals Expression and Characterization of the Small Subunit of Human DNA Polymerase δ

1997 ◽  
Vol 272 (20) ◽  
pp. 13013-13018 ◽  
Author(s):  
Yubo Sun ◽  
Yunquan Jiang ◽  
Peng Zhang ◽  
Shan-Jian Zhang ◽  
Yi Zhou ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Small Subunit ◽  
Dna Polymerase Δ ◽  
Human Dna

scholarly journals Reconstitution of Human DNA Polymerase δ Using Recombinant Baculoviruses

2001 ◽  
Vol 277 (6) ◽  
pp. 3894-3901 ◽  
Author(s):  
Vladimir N. Podust ◽  
Long-Sheng Chang ◽  
Robert Ott ◽  
Grigory L. Dianov ◽  
Ellen Fanning
Keyword(s):  
Dna Polymerase ◽  
Recombinant Baculoviruses ◽  
Dna Polymerase Δ ◽  
Human Dna

scholarly journals Expression of the Catalytic Subunit of Human DNA Polymerase δ in Mammalian Cells Using a Vaccinia Virus Vector System

1995 ◽  
Vol 270 (14) ◽  
pp. 7993-7998 ◽  
Author(s):  
Peng Zhang ◽  
Isabelle Frugulhetti ◽  
Yunquan Jiang ◽  
Geraldine L. Holt ◽  
Richard C. Condit ◽  
...  
Keyword(s):  
Vaccinia Virus ◽  
Dna Polymerase ◽  
Mammalian Cells ◽  
Virus Vector ◽  
Catalytic Subunit ◽  
Vector System ◽  
Dna Polymerase Δ ◽  
Human Dna ◽  
Vaccinia Virus Vector
Sign in / Sign up

Export Citation Format

Share Document