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Genetics, Vol 127, 61-73, Copyright © 1991
INVESTIGATIONS |
A Novel Recombinator in Yeast Based on Gene II Protein from Bacteriophage f1
J. N. Strathern, K. G. Weinstock, D. R. Higgins and C. B. McGill
Laboratory of Eukaryotic Gene Expression, NCI-Frederick Cancer Research and Development Center, Basic Research Program, Frederick, Maryland 21702-1201
Interchromosomal mitotic recombination in yeast can be stimulated by the protein encoded by gene II of bacteriophage f1. The normal role of the gene II enzyme is to make a site-specific cleavage of a particular strand of the duplex form of the bacteriophage DNA at the origin of DNA replication. The gene II protein was expressed in yeast in an attempt to determine the role of nicked DNA in the initiation of recombination. Stimulation of recombination in yeast by the gene II protein was dependent on the presence of a recognition site for gene II enzyme in the region being assayed. Recombination was stimulated in both directions from the gene II recognition site but showed a directional bias. The distribution of alleles among the recombinants indicated that the chromosome with the gene II recognition site acted as the recipient in gene conversion events.
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