Characterization of the POL3 gene product from Schizosaccharomyces pombe indicates inter-species conservation of the catalytic subunit of DNA polymerase δ

Pignède, Georges; Bouvier, Dominique; Recondo, Anne-Marie de; Baldacci, Giuseppe

doi:10.1016/0022-2836(91)90207-m

Cited by 42 publications

(23 citation statements)

References 27 publications

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“…The coding sequence of the pol3' gene encodes a protein of 1086 amino acids with a predicted molecular weight of 123 985 Da. The predicted amino acid sequence of polb+ gene isolated by us revealed several discrepancies from that reported by Pignede et al (1991). Our DNA polymerase 6 sequence has Q102 and T419 in contrast to E102 and S4"9.…”

Section: Resultscontrasting

confidence: 46%

“…Our DNA polymerase 6 sequence has Q102 and T419 in contrast to E102 and S4"9. In addition to these differences, our predicted amino acid sequence from the residue 777 to 784 showed KLEFEKVY containing two additional amino acids, which was entirely different from the sequence NWSF-T-in this region reported by Pignede et al (1991). It is possible that the differences in these amino acid residues are due to a genetic heterogeneity of the S. pombe strains from which the genomic DNAs were originally isolated.…”

Section: Resultsmentioning

confidence: 67%

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Cell cycle expression of two replicative DNA polymerases alpha and delta from Schizosaccharomyces pombe.

Park

Francesconi

Wang

1993

MBoC

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We have investigated the expression of two Schizosaccharomyces pombe replicative DNA polymerases a and 6 during the cell cycle. The pola' and pol6+ genes encoding DNA polymerases a and 6 were isolated from S. pombe. Both pola' and pol6+ genes are single copy genes in haploid cells and are essential for cell viability. In contrast to Saccharomyces cerevisiae homologs, the steady-state transcripts of both S. pombe pola' and pol6+ genes were present throughout the cell cycle. Sequence analysis of the pola' and pol6+ genes did not reveal the Mlu I motifs in their upstream sequences that are involved in cell cycledependent transcription of S. cerevisiae DNA synthesis genes as well as the S. pombe cdc22+ gene at the G1/S boundary. However, five near-match Mlu I motifs were found in the upstream region of the pola' gene. S. pombe DNA polymerases a and 6 proteins were also expressed constantly throughout the cell cycle. In addition, the enzymatic activity of the S. pombe DNA polymerase a measured by in vitro assay was detected at all stages of the cell cycle. Thus, these S. pombe replicative DNA polymerases, like that of S. pombe cdc17+ gene, are expressed throughout the cell cycle at the transcriptional and protein level. These results indicate that S. pombe has at least two regulatory modes for the expression of genes involved in DNA replication and DNA precursor synthesis.

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Section: Resultscontrasting

confidence: 46%

Section: Resultsmentioning

confidence: 67%

Cell cycle expression of two replicative DNA polymerases alpha and delta from Schizosaccharomyces pombe.

Park

Francesconi

Wang

1993

MBoC

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“…p125 is the catalytic subunit for both DNA polymerase activity and a proofreading, 3 -5 exonuclease activity. cDNAs for each subunit have been cloned (175)(176)(177)(178)(179)(180)(181)(182)(183). Moreover, an active human dimeric complex has been reconstituted using proteins expressed in recombinant baculovirus-infected insect cells (184).…”

Section: Dna Polymerases δ and εmentioning

confidence: 99%

The Dna Replication Fork in Eukaryotic Cells

Waga

Stillman

1998

Annu. Rev. Biochem.

739

653

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Replication of the two template strands at eukaryotic cell DNA replication forks is a highly coordinated process that ensures accurate and efficient genome duplication. Biochemical studies, principally of plasmid DNAs containing the Simian Virus 40 origin of DNA replication, and yeast genetic studies have uncovered the fundamental mechanisms of replication fork progression. At least two different DNA polymerases, a single-stranded DNA-binding protein, a clamp-loading complex, and a polymerase clamp combine to replicate DNA. Okazaki fragment synthesis involves a DNA polymerase-switching mechanism, and maturation occurs by the recruitment of specific nucleases, a helicase, and a ligase. The process of DNA replication is also coupled to cell-cycle progression and to DNA repair to maintain genome integrity. CONTENTS

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“…The POL3 and POL31 (HYS2) genes are essential, but the POL32 gene is dispensable, although deletion mutants show defects in DNA replication, DNA repair, and mutagenesis (8 -11). The enzyme from Schizosaccharomyces pombe consists of four subunits: Pol3, Cdc1 (the ortholog of Pol31), Cdc27 (the ortholog of Pol32), and Cdm1 (12)(13)(14)(15). The genes for the three large subunits are essential, but a deletion of the Cdm1 ϩ gene, a homologue of which has not been identified in S. cerevisiae, shows no phenotype in the absence of mutations in the Cdc1 ϩ gene (16).…”

Section: Dna Polymerase ␦ (Pol ␦)mentioning

confidence: 99%

Structure of DNA Polymerase δ from Saccharomyces cerevisiae

Johansson¹,

Majka

Burgers³

2001

Journal of Biological Chemistry

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DNA polymerase ␦ (Pol ␦) from Saccharomyces cerevisiae consists of three subunits, Pol3 (125 kDa), Pol31 (55 kDa), and Pol32 (40 kDa), present at a 1:1:1 stoichiometry in purified preparations. Previously, based on gel filtration studies of Pol ␦, we suggested that the enzyme may be a dimer of catalytic cores, with dimerization mediated by the Pol32 subunit (Burgers, P. M., and Gerik, K. J. (1998) J. Biol. Chem. 273, 19756 -19762). We now report on extensive gel filtration, glycerol gradient sedimentation, and analytical equilibrium centrifugation studies of Pol ␦ and of several subassemblies of Pol ␦. The hydrodynamic parameters of these assemblies indicate that (i) Pol32 is a rod-shaped protein with a frictional ratio f/f 0 ‫؍‬ 2.22; (ii) any complex containing Pol32 also has an extremely asymmetric shape; (iii) the results of these studies are independent of concentration (varied between 0.1-20 M); (iv) all complexes are monomeric under the conditions studied (up to 20 M). Moreover, a two-hybrid analysis of the Pol32 subunit did not detect a Pol32-Pol32 interaction in vivo. Therefore, we conclude that the assembly structure of Pol ␦ is that of a monomer.

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Characterization of the POL3 gene product from Schizosaccharomyces pombe indicates inter-species conservation of the catalytic subunit of DNA polymerase δ

Cited by 42 publications

References 27 publications

Cell cycle expression of two replicative DNA polymerases alpha and delta from Schizosaccharomyces pombe.

Cell cycle expression of two replicative DNA polymerases alpha and delta from Schizosaccharomyces pombe.

The Dna Replication Fork in Eukaryotic Cells

Structure of DNA Polymerase δ from Saccharomyces cerevisiae

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