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Multi‐functional DNA proteins in yeast: The factors GFI and GFII are identical to the ARS‐binding factor ABFI and the centromere‐binding factor CPF1 respectively
Author(s) -
Dorsman J. C.,
GozdzickaJozefiak A.,
Van Heeswijk W. C.,
Grivell L. A.
Publication year - 1991
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320070410
Subject(s) - biology , yeast , saccharomyces cerevisiae , centromere , dna , biochemistry , dna binding protein , binding protein , mutant , microbiology and biotechnology , binding site , proteolysis , genetics , transcription factor , gene , enzyme , chromosome
Abstract GFI and GFII are abundant DNA‐binding proteins in the yeast Saccharomyces cerevisiae . Binding sites for GFI conform to the sequence 5′‐RTCRYACG‐3′. This consensus can also accommodate the recognition sequence for the ARS1 ‐binding factor ABFI. Results of retardation‐competition assays, limited proteolysis experiments, molecular weight determinations based on denaturation–renaturation procedures and mobility shift assays of protein–DNA complexes formed in the presence of a monoclonal antibody raised against ABFI suggest strongly that GFI and ABFI are the same protein. Similarly, GFII appears to be identical to the centromere‐binding protein CPFI (alias CP1), since both proteins bind to the CDEI motif of yeast centromeres (5′‐RTCACRTG‐3′) and cannot be detected in a cpf1 disruption mutant yeast strain. In addition, based on denaturation–renaturation studies, both factors appear to have molecular weights in the same range of 53–62 kDa.