DNA polymerase delta isolated from Schizosaccharomyces pombe contains five subunits

SJ Zuo, E Gibbs, Z Kelman, TSF Wang, M ODonnell, Stuart Andrew MacNeill, J Hurwitz

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73 Citations (Scopus)

Abstract

DNA polymerase delta (pol delta) plays an essential role in DNA replication, repair, and recombination. We have purified pol delta from Schizosaccharomyces pombe more than 10(3)-fold and demonstrated that the polymerase activity of purified S. pombe pol delta is completely dependent on proliferating cell nuclear antigen and replication factor C. SDS/PAGE analysis of the purified fraction indicated that the pol delta complex consists of Five subunits that migrate with apparent molecular masses of 125, 55, 54, 42, and 22 kDa. Western blot analysis indicated that the 125, 55, and 54 kDa proteins are the large catalytic subunit (Pol3), Cdc1, and Cdc37, respectively. The identity of the other two subunits, p42 and p22, was determined following proteolytic digestion and sequence analysis of the resulting peptides. The peptide sequences derived from the p22 subunit indicated that this subunit is identical to Cdm1, previously identified as a multicopy suppressor of the temperature-sensitive cdc1-P13 mutant, whereas peptide sequences derived from the p42 subunit were identical to a previously uncharacterized ORF located on S. pombe chromosome 1.

Original languageEnglish
Pages (from-to)11244-11249
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number21
DOIs
Publication statusPublished - 14 Oct 1997

Keywords

  • CELL NUCLEAR ANTIGEN
  • SACCHAROMYCES-CEREVISIAE
  • CATALYTIC SUBUNIT
  • FISSION YEAST
  • MOLECULAR-CLONING
  • REPLICATION FORK
  • SEQUENCE-ANALYSIS
  • GENE
  • PURIFICATION
  • INVITRO

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