Open AccessDNA polymerase I gene of Saccharomyces cerevisiae: nucleotide sequence, mapping of a temperature-sensitive mutation, and protein homology with other DNA polymerases.
Author(s) -
Antonella Pizzagalli,
Paola Valsasnini,
Paolo Plevani,
Giovanna Lucchini
Publication year - 1988
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.85.11.3772
Subject(s) - dna polymerase , biology , polymerase , dna clamp , dna polymerase ii , genetics , primase , dna polymerase i , base pair , microbiology and biotechnology , dna polymerase mu , nucleic acid sequence , gene , biochemistry , circular bacterial chromosome , polymerase chain reaction , reverse transcriptase
A 5600-base pair segment spanning the coding region of the Saccharomyces cerevisiae DNA polymerase I gene was sequenced and found to contain an open reading frame of 1468 codons, corresponding to a polypeptide of Mr 166,794. A pol1 temperature-sensitive mutation, encoding a DNA-polymerase-primase complex with altered stability, has a single base-pair substitution that changes the glycine at position 493 to a positively charged arginine. Protein sequence comparison with other prokaryotic and eukaryotic DNA polymerases reveals three major regions of homology. This observation suggests that certain DNA polymerases might require the conservation of critical amino acid residues for activity.