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dc.contributor.authorMasison, Daniel C.
dc.contributor.authorO'Connell, Kevin F.
dc.contributor.authorBaker, Richard E.
dc.date2022-08-11T08:09:01.000
dc.date.accessioned2022-08-23T16:15:42Z
dc.date.available2022-08-23T16:15:42Z
dc.date.issued1993-08-25
dc.date.submitted2008-11-05
dc.identifier.citationNucleic Acids Res. 1993 Aug 25;21(17):4133-41. <a href="http://dx.doi.org/10.1093/nar/21.17.4133">Link to article on publisher's website</a>
dc.identifier.issn0305-1048 (Print)
dc.identifier.doi10.1093/nar/21.17.4133
dc.identifier.pmid8371988
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34154
dc.description.abstractThe 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.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8371988&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://nar.oxfordjournals.org/cgi/content/abstract/21/17/4133
dc.subjectAlleles; 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
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleMutational analysis of the Saccharomyces cerevisiae general regulatory factor CP1
dc.typeArticle
dc.source.journaltitleNucleic acids research
dc.source.volume21
dc.source.issue17
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1813&amp;context=gsbs_sp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/814
dc.identifier.contextkey661924
refterms.dateFOA2022-08-23T16:15:43Z
html.description.abstract<p>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.</p>
dc.identifier.submissionpathgsbs_sp/814
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages4133-41


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