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    Mutational analysis of the Saccharomyces cerevisiae general regulatory factor CP1

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    Authors
    Masison, Daniel C.
    O'Connell, Kevin F.
    Baker, Richard E.
    UMass Chan Affiliations
    Department of Molecular Genetics and Microbiology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    1993-08-25
    Keywords
    Alleles; Base Sequence; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors; DNA Mutational Analysis; DNA, Fungal; DNA-Binding Proteins; Frameshift Mutation; Fungal Proteins; Molecular Sequence Data; Mutagenesis; Phenotype; Saccharomyces cerevisiae; *Saccharomyces cerevisiae Proteins; Transformation, Genetic
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://nar.oxfordjournals.org/cgi/content/abstract/21/17/4133
    Abstract
    The Saccharomyces cerevisiae general regulatory factor CP1, a helix-loop-helix protein that binds the centromere DNA element I (CDEI) of yeast centromeres, is required in yeast for optimal centromere function and for methionine prototrophy. Mutant alleles of CEP1, the gene encoding CP1, were generated by linker insertion, 5'- and 3'-deletion, and random mutagenesis and assayed for DNA binding activity and their ability to confer CP1 function when expressed in yeast. A heterologous CDEI-binding protein, TFEB, was also tested for CP1 function. The results suggested that DNA binding is required for both biological functions of CP1 but is not sufficient. A direct and quantitative correlation was observed between the chromosome loss and nutritional (i.e., Met) phenotypes of strains carrying loss of function alleles, but qualitatively the chromosome loss phenotype was more sensitive to decreased CP1 expression. The data are consistent with a model in which CP1 performs the same general chromatin-related function at centromeres and MET gene promoters and is normally present in functional excess.
    Source
    Nucleic Acids Res. 1993 Aug 25;21(17):4133-41. Link to article on publisher's website
    DOI
    10.1093/nar/21.17.4133
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/34154
    PubMed ID
    8371988
    Related Resources
    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1093/nar/21.17.4133
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    Morningside Graduate School of Biomedical Sciences Scholarly Publications

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