scholarly journals Direct Interaction of p21 with p50, the Small Subunit of Human DNA Polymerase Delta

Cell Cycle ◽  
2006 ◽  
Vol 5 (4) ◽  
pp. 428-436 ◽  
Author(s):  
Hao Li ◽  
Bin Xie ◽  
Amal Rahmeh ◽  
Yajing Zhou ◽  
Marietta Y.W.T. Lee
Keyword(s):  
Dna Polymerase ◽  
Direct Interaction ◽  
Small Subunit ◽  
Dna Polymerase Delta ◽  
Human Dna

scholarly journals Regulation of human DNA polymerase delta during the cell cycle.

1994 ◽  
Vol 269 (39) ◽  
pp. 24027-24033
Author(s):  
X.R. Zeng ◽  
H. Hao ◽  
Y. Jiang ◽  
M.Y. Lee
Keyword(s):  
Cell Cycle ◽  
Dna Polymerase ◽  
Dna Polymerase Delta ◽  
Human Dna

scholarly journals The fission yeast Cdc1 protein, a homologue of the small subunit of DNA polymerase delta, binds to Pol3 and Cdc27.

1996 ◽  
Vol 15 (17) ◽  
pp. 4613-4628 ◽  
Author(s):  
S. A. MacNeill ◽  
S. Moreno ◽  
N. Reynolds ◽  
P. Nurse ◽  
P. A. Fantes
Keyword(s):  
Fission Yeast ◽  
Dna Polymerase ◽  
Protein A ◽  
Small Subunit ◽  
Dna Polymerase Delta

scholarly journals Conditional mutations in the yeast DNA primase genes affect different aspects of DNA metabolism and interactions in the DNA polymerase alpha-primase complex.

Genetics ◽  
1993 ◽  
Vol 133 (2) ◽  
pp. 183-191 ◽  
Author(s):  
M P Longhese ◽  
L Jovine ◽  
P Plevani ◽  
G Lucchini
Keyword(s):  
Dna Polymerase ◽  
Large Subunit ◽  
Spontaneous Mutation ◽  
Critical Role ◽  
Direct Interaction ◽  
Small Subunit ◽  
Dna Polymerase Alpha ◽  
Dna Primase ◽  
Primase Complex

Abstract Different pri1 and pri2 conditional mutants of Saccharomyces cerevisiae altered, respectively, in the small (p48) and large (p58) subunits of DNA primase, show an enhanced rate of both mitotic intrachromosomal recombination and spontaneous mutation, to an extent which is correlated with the severity of their defects in cell growth and DNA synthesis. These effects might be attributable to the formation of nicked and gapped DNA molecules that are substrates for recombination and error-prone repair, due to defective DNA replication in the primase mutants. Furthermore, pri1 and pri2 mutations inhibit sporulation and affect spore viability, with the unsporulated mutant cells arresting with a single nucleus, suggesting that DNA primase plays a critical role during meiosis. The observation that all possible pairwise combinations of two pri1 and two pri2 alleles are lethal provides further evidence for direct interaction of the primase subunits in vivo. Immunopurification and immunoprecipitation studies on wild-type and mutant strains suggest that the small subunit has a major role in determining primase activity, whereas the large subunit directly interacts with DNA polymerase alpha, and either mediates or stabilizes association of the p48 polypeptide in the DNA polymerase alpha-primase complex.

scholarly journals Human DNA polymerase delta is a pentameric holoenzyme with dimeric p12 subunit: Implications in enzyme architecture and PCNA interaction

2019 ◽  
Author(s):  
Prashant Khandagale ◽  
Doureradjou Peroumal ◽  
Kodavati Manohar ◽  
Narottam Acharya
Keyword(s):  
Dna Replication ◽  
Dna Polymerase ◽  
Essential Role ◽  
Amino Terminus ◽  
Dna Polymerase Delta ◽  
Human Dna ◽  
Evolutionarily Conserved ◽  
Carboxyl Terminal

AbstractHuman DNA polymerase delta (Polδ), a holoenzyme consisting of p125, p50, p68 and p12 subunits, plays an essential role in all the three DNA transaction processes. Herein, using multiple physicochemical and cellular approaches we found that the p12 protein forms a dimer in solution. In vitro reconstitution and pull-down of cellular Polδ by tagged p12 authenticates pentameric nature of this critical holoenzyme. Further, a consensus PIP motif at the extreme carboxyl terminal tail and a homodimerization domain at the amino-terminus of the p12 subunit were identified. Our mutational analyses of p12 subunit suggest that 3RKR5 motif is critical for dimerization that facilitates p12 binding to IDCL of PCNA via its PIP motif 98QCSLWHLY105. Additionally, we observed that oligomerization of the smallest subunit of Polδs is evolutionarily conserved as Cdm1 of S. pombe also dimerzes. Thus, we suggest that human Polδ is a pentameric complex with a dimeric p12 subunit; and discuss implications of p12 dimerization in regulating enzyme architecture and PCNA interaction during DNA replication.

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 Human DNA polymerase delta double-mutant D316A;E318A interferes with DNA mismatch repair in vitro

2017 ◽  
Vol 45 (16) ◽  
pp. 9427-9440 ◽  
Author(s):  
Dekang Liu ◽  
Jane H. Frederiksen ◽  
Sascha E. Liberti ◽  
Anne Lützen ◽  
Guido Keijzers ◽  
...  
Keyword(s):  
Mismatch Repair ◽  
Dna Polymerase ◽  
Double Mutant ◽  
Dna Mismatch Repair ◽  
Dna Polymerase Delta ◽  
Dna Mismatch ◽  
Human Dna

scholarly journals P50, the Small Subunit of DNA Polymerase Delta, Is Required for Mediation of the Interaction of Polymerase Delta Subassemblies with PCNA

PLoS ONE ◽  
2011 ◽  
Vol 6 (11) ◽  
pp. e27092 ◽  
Author(s):  
Yujue Wang ◽  
Qian Zhang ◽  
Huiqing Chen ◽  
Xiao Li ◽  
Weijun Mai ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Small Subunit ◽  
Dna Polymerase Delta

scholarly journals Primary structure of the catalytic subunit of human DNA polymerase delta and chromosomal location of the gene.

1991 ◽  
Vol 88 (24) ◽  
pp. 11197-11201 ◽  
Author(s):  
D. W. Chung ◽  
J. A. Zhang ◽  
C. K. Tan ◽  
E. W. Davie ◽  
A. G. So ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Primary Structure ◽  
Chromosomal Location ◽  
Catalytic Subunit ◽  
Dna Polymerase Delta ◽  
Human Dna
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