scholarly journals The small subunit of DNA polymerase D (DP1) associates with GINS–GAN complex of the thermophilic archaea inThermococcussp. 4557

2019 ◽  
Vol 8 (9) ◽  
Author(s):  
Shuhong Lu ◽  
Xuesong Zhang ◽  
Kaiying Chen ◽  
Zimeng Chen ◽  
Yixiang Li ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Small Subunit ◽  
Thermophilic Archaea

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 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 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 Archaeal DNA Replication: Identifying the Pieces to Solve a Puzzle

Genetics ◽  
1999 ◽  
Vol 152 (4) ◽  
pp. 1249-1267 ◽  
Author(s):  
Isaac K O Cann ◽  
Yoshizumi Ishino
Keyword(s):  
Dna Replication ◽  
Dna Polymerase ◽  
Pyrococcus Furiosus ◽  
Sequence Similarity ◽  
Large Subunit ◽  
Dna Polymerases ◽  
Small Subunit ◽  
Accessory Proteins ◽  
Pol Ii

Abstract Archaeal organisms are currently recognized as very exciting and useful experimental materials. A major challenge to molecular biologists studying the biology of Archaea is their DNA replication mechanism. Undoubtedly, a full understanding of DNA replication in Archaea requires the identification of all the proteins involved. In each of four completely sequenced genomes, only one DNA polymerase (Pol BI proposed in this review from family B enzyme) was reported. This observation suggested that either a single DNA polymerase performs the task of replicating the genome and repairing the mutations or these genomes contain other DNA polymerases that cannot be identified by amino acid sequence. Recently, a heterodimeric DNA polymerase (Pol II, or Pol D as proposed in this review) was discovered in the hyperthermophilic archaeon, Pyrococcus furiosus. The genes coding for DP1 and DP2, the subunits of this DNA polymerase, are highly conserved in the Euryarchaeota. Euryarchaeotic DP1, the small subunit of Pol II (Pol D), has sequence similarity with the small subunit of eukaryotic DNA polymerase δ. DP2 protein, the large subunit of Pol II (Pol D), seems to be a catalytic subunit. Despite possessing an excellent primer extension ability in vitro, Pol II (Pol D) may yet require accessory proteins to perform all of its functions in euryarchaeotic cells. This review summarizes our present knowledge about archaeal DNA polymerases and their relationship with those accessory proteins, which were predicted from the genome sequences.

scholarly journals DNA polymerase η is a substrate for calpain: A possible mechanism for pol η retention in UV induced replication foci

2021 ◽  
Author(s):  
Jo-Ann Nettersheim ◽  
Régine Janel-Bintz ◽  
Lauriane Kuhn ◽  
Agnès M Cordonnier
Keyword(s):  
Dna Polymerase ◽  
Calcium Ionophore ◽  
Small Subunit ◽  
Dna Lesions ◽  
Calpain Inhibitor ◽  
Translesion Dna Synthesis ◽  
Calcium Dependent ◽  
Catalytically Active ◽  
Radiation Induced ◽  
Replication Foci

DNA polymerase η (pol η) is specifically required for translesion DNA synthesis across ultraviolet radiation-induced DNA lesions. Recruitment of this error-prone DNA polymerase is tightly regulated during replication to avoid mutagenesis and perturbation of fork progression. Here we report that pol η interacts with the calpain small subunit-1 (CAPNS1), in a yeast two-hybrid screening. This interaction is functional as demonstrated by the ability of endogenous calpain to mediate calcium-dependent cleavage of pol η in cell-free extracts and in living cells treated with a calcium ionophore. The proteolysis of pol η is found to occur at position 465 leading to a catalytically active truncated protein containing the PCNA-interacting motif PIP1. Unexpectedly, cell treatment with the specific calpain inhibitor calpeptin results in a decreased extent of pol η foci after UV irradiation, indicating that calpain positively regulates pol η accumulation in replication foci.

scholarly journals Direct Interaction of Proliferating Cell Nuclear Antigen with the Small Subunit of DNA Polymerase δ

2002 ◽  
Vol 277 (27) ◽  
pp. 24340-24345 ◽  
Author(s):  
Xiaoqing Lu ◽  
Cheng-Keat Tan ◽  
Jin-Qiu Zhou ◽  
Min You ◽  
L. Michael Carastro ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Proliferating Cell Nuclear Antigen ◽  
Direct Interaction ◽  
Small Subunit ◽  
Nuclear Antigen ◽  
Dna Polymerase Δ ◽  
Proliferating Cell

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
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