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dc.contributor.authorVan Wijnen, Andre J.
dc.contributor.authorLian, Jane B.
dc.contributor.authorStein, Janet L.
dc.contributor.authorStein, Gary S.
dc.date2022-08-11T08:08:50.000
dc.date.accessioned2022-08-23T16:09:35Z
dc.date.available2022-08-23T16:09:35Z
dc.date.issued1991-12-01
dc.date.submitted2009-01-13
dc.identifier.citationJ Cell Biochem. 1991 Dec;47(4):337-51. <a href="http://dx.doi.org/10.1002/jcb.240470408">Link to article on publisher's site</a>
dc.identifier.issn0730-2312 (Print)
dc.identifier.doi10.1002/jcb.240470408
dc.identifier.pmid1795016
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32732
dc.description.abstractProtein/DNA interactions of the H3-ST519 histone gene promoter were analyzed in vitro. Using several assays for sequence specificity, we established binding sites for ATF/AP1-, CCAAT-, and HiNF-D related DNA binding proteins. These binding sites correlate with two genomic protein/DNA interaction domains previously established for this gene. We show that each of these protein/DNA interactions has a counterpart in other histone genes: H3-ST519 and H4-F0108 histone genes interact with ATF- and HiNF-D related binding activities, whereas H3-ST519 and H1-FNC16 histone genes interact with the same CCAAT-box binding activity. These factors may function in regulatory coupling of the expression of different histone gene classes. We discuss these results within the context of established and putative protein/DNA interaction sites in mammalian histone genes. This model suggests that heterogeneous permutations of protein/DNA interaction elements, which involve both general and cell cycle regulated DNA binding proteins, may govern the cellular competency to express and coordinately control multiple distinct histone genes.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=1795016&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1002/jcb.240470408
dc.subjectActivating Transcription Factors; Base Sequence; Binding Sites; Binding, Competitive; Blood Proteins; CCAAT-Enhancer-Binding Proteins; Cell Cycle; DNA; DNA Fingerprinting; DNA Probes; DNA-Binding Proteins; Deoxyribonuclease I; *Gene Expression Regulation; Histones; Humans; Methylation; Molecular Sequence Data; *Promoter Regions (Genetics); Sulfuric Acid Esters; Transcription Factors; Transcription, Genetic
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleProtein/DNA interactions involving ATF/AP1-, CCAAT-, and HiNF-D-related factors in the human H3-ST519 histone promoter: cross-competition with transcription regulatory sites in cell cycle controlled H4 and H1 histone genes
dc.typeJournal Article
dc.source.journaltitleJournal of cellular biochemistry
dc.source.volume47
dc.source.issue4
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1288
dc.identifier.contextkey693217
html.description.abstract<p>Protein/DNA interactions of the H3-ST519 histone gene promoter were analyzed in vitro. Using several assays for sequence specificity, we established binding sites for ATF/AP1-, CCAAT-, and HiNF-D related DNA binding proteins. These binding sites correlate with two genomic protein/DNA interaction domains previously established for this gene. We show that each of these protein/DNA interactions has a counterpart in other histone genes: H3-ST519 and H4-F0108 histone genes interact with ATF- and HiNF-D related binding activities, whereas H3-ST519 and H1-FNC16 histone genes interact with the same CCAAT-box binding activity. These factors may function in regulatory coupling of the expression of different histone gene classes. We discuss these results within the context of established and putative protein/DNA interaction sites in mammalian histone genes. This model suggests that heterogeneous permutations of protein/DNA interaction elements, which involve both general and cell cycle regulated DNA binding proteins, may govern the cellular competency to express and coordinately control multiple distinct histone genes.</p>
dc.identifier.submissionpathgsbs_sp/1288
dc.contributor.departmentDepartment of Cell Biology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages337-51


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