Open AccessMolecular genetic studies of the Cdc7 protein kinase and induced mutagenesis in yeast.
Author(s) -
Robert E. Hollingsworth,
Rachel Ostroff,
Michael Klein,
Lee Niswander,
Robert A. Sclafani
Publication year - 1992
Publication title -
genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.792
H-Index - 246
eISSN - 1943-2631
pISSN - 0016-6731
DOI - 10.1093/genetics/132.1.53
Subject(s) - biology , mutagenesis , insertional mutagenesis , genetics , dna repair , mutant , mutation , chromatin , saccharomyces cerevisiae , protein kinase a , homologous recombination , site directed mutagenesis , dna replication , gene , microbiology and biotechnology , kinase
The Saccharomyces cerevisiae CDC7 gene encodes a protein kinase that functions in DNA replication, repair, and meiotic recombination. The sequence of several temperature-sensitive (ts) cdc7 mutations was determined and correlated with protein kinase consensus domain structure. The positions of these ts alleles suggests some general principles for predicting ts protein kinase mutations. Pedigree segregation lag analysis demonstrated that all of the mutant proteins are less active or less stable than wild-type Cdc7p. Two new mutations were constructed, one by site-directed and the other by insertional mutagenesis. All of the cdc7 mutants were assayed for induced mutagenesis in response to mutagenic agents at the permissive temperature. Some cdc7 mutants were found to be hypomutable, while others are hypermutable. The differences in mutability are observed most clearly when log phase cells are used. Both hypo- and hypermutability are recessive to wild type. Cdc7p may participate in DNA repair by phosphorylating repair enzymes or by altering chromatin structure to allow accessibility to DNA lesions.