Open AccessCharacteristic alteration in the nuclear DNA polymerase activity during the cell division cycle ofSaccharomyces cerevisiae
Author(s) -
Eiko Tsuchiya,
Kosei Kimura,
Tokichi Miyakawa,
Sakuzô Fukui
Publication year - 1984
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/12.7.3143
Subject(s) - biology , dna polymerase , cell cycle , microbiology and biotechnology , saccharomyces cerevisiae , polymerase , protein subunit , cell division , dna synthesis , mutant , s phase , dna , dna replication , nuclear dna , biochemistry , cell , eukaryotic dna replication , gene , mitochondrial dna
Specific activity of the intranuclear DNA polymerase in cdc-mutant cells of Saccharomyces cerevisiae was found to be characteristically changed by arrest in their specific stage of cell division cycle without a notable alteration in the total cellular activity. The activities were low in the nuclei of cdc 25, cdc 28 and cdc 4, which were arrested in early to mid G1 phase by temperature shift-up, and in the nuclei of wild-type cells (A364A), which were arrested in early G1 phase by alpha-factor treatment, while high level of the activity was found in the nuclei of cdc 7 and cdc 8, which were arrested at late G1 and S phase, respectively. Activity-gel analysis of DNA polymerase in the nuclear extracts revealed the presence of two active peptides (120K and 72K), and the characteristic decrease in both active peptides was induced by arrest in early to mid G1 phase. Consequently, it is strongly suggested that intranuclear DNA polymerase activity alters in a dependent fashion on progression of cell division cycle. Subunit analysis indicated that the purified DNA polymerase I is constructed from two subunit peptides of 120K and 62K, and the large subunit possesses catalytic activity.