The Pol32 Subunit of DNA Polymerase δ Contains Separable Domains for Processive Replication and Proliferating Cell Nuclear Antigen (PCNA) Binding (Q79241756)

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scientific article published on October 31, 2003

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English	The Pol32 Subunit of DNA Polymerase δ Contains Separable Domains for Processive Replication and Proliferating Cell Nuclear Antigen (PCNA) Binding	scientific article published on October 31, 2003

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20 December 2019

The Pol32 subunit of DNA polymerase delta contains separable domains for processive replication and proliferating cell nuclear antigen (PCNA) binding (English)

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20 December 2019

The Pol32 Subunit of DNA Polymerase δ Contains Separable Domains for Processive Replication and Proliferating Cell Nuclear Antigen (PCNA) Binding (English)

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10.1074/JBC.M310362200

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27 March 2024

DNA replication

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27 March 2024

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27 March 2024

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27 March 2024

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Erik Johansson

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27 March 2024

author name string

Parie Garg

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20 December 2019

Peter M. J. Burgers

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27 March 2024

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31 October 2003

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20 December 2019

full work available at URL

http://www.jbc.org/content/279/3/1907.full.pdf

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27 March 2024

https://api.elsevier.com/content/article/PII:S0021925820687518?httpAccept=text/xml

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27 March 2024

https://api.elsevier.com/content/article/PII:S0021925820687518?httpAccept=text/plain

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10.1074/JBC.M310362200

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27 March 2024

https://syndication.highwire.org/content/doi/10.1074/jbc.M310362200

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27 March 2024

Journal of Biological Chemistry

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20 December 2019

279

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20 December 2019

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20 December 2019

1907-1915

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20 December 2019

Eukaryotic DNA polymerases in DNA replication and DNA repair

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DNA polymerase epsilon catalytic domains are dispensable for DNA replication, DNA repair, and cell viability

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Analysis of the essential functions of the C-terminal protein/protein interaction domain of Saccharomyces cerevisiae pol epsilon and its unexpected ability to support growth in the absence of the DNA polymerase domain

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The DNA polymerase domain of pol(epsilon) is required for rapid, efficient, and highly accurate chromosomal DNA replication, telomere length maintenance, and normal cell senescence in Saccharomyces cerevisiae

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Evidence from mutational specificity studies that yeast DNA polymerases delta and epsilon replicate different DNA strands at an intracellular replication fork

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Yeast origins establish a strand bias for replicational mutagenesis.

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Characterization of the two small subunits of Saccharomyces cerevisiae DNA polymerase delta

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DNA polymerase δ isolated from Schizosaccharomyces pombe contains five subunits

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Identification of a fourth subunit of mammalian DNA polymerase delta

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Reconstitution of human DNA polymerase delta using recombinant baculoviruses: the p12 subunit potentiates DNA polymerizing activity of the four-subunit enzyme

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Cdm1, the smallest subunit of DNA polymerase d in the fission yeast Schizosaccharomyces pombe, is non-essential for growth and division

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Surveying Saccharomyces genomes to identify functional elements by comparative DNA sequence analysis.

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Structure of DNA polymerase delta from Saccharomyces cerevisiae

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The Influence of the Cdc27 Subunit on the Properties of theSchizosaccharomyces pombeDNA Polymerase δ

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Essential interaction between the fission yeast DNA polymerase delta subunit Cdc27 and Pcn1 (PCNA) mediated through a C-terminal p21(Cip1)-like PCNA binding motif

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Lagging Strand DNA Synthesis at the Eukaryotic Replication Fork Involves Binding and Stimulation of FEN-1 by Proliferating Cell Nuclear Antigen

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The Saccharomyces cerevisiae protein YJR043C (Pol32) interacts with the catalytic subunit of DNA polymerase alpha and is required for cell cycle progression in G2/M

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POL32, a subunit of the Saccharomyces cerevisiae DNA polymerase delta, defines a link between DNA replication and the mutagenic bypass repair pathway

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Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA replication through a conserved p21(Cip1)-like PCNA-binding motif present in the third subunit of human DNA polymerase delta

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A conserved region in the amino terminus of DNA polymerase delta is involved in proliferating cell nuclear antigen binding

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Direct interaction of proliferating cell nuclear antigen with the p125 catalytic subunit of mammalian DNA polymerase delta

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The human homologue of fission Yeast cdc27, p66, is a component of active human DNA polymerase delta

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Direct interaction of proliferating cell nuclear antigen with the small subunit of DNA polymerase delta

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PCNA and DNA polymerase delta catalytic subunit from Schizosaccharomyces pombe do not interact directly

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Two modes of FEN1 binding to PCNA regulated by DNA.

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Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA

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Identifiers

10.1074/JBC.M310362200

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14594808%20AND%20SRC:MED&resulttype=core&format=json

20 December 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14594808%20AND%20SRC:MED&resulttype=core&format=json

20 December 2019

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