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dc.contributor.authorLast, Thomas J.
dc.contributor.authorVan Wijnen, Andre J.
dc.contributor.authorBirnbaum, Mark J.
dc.contributor.authorStein, Gary S.
dc.contributor.authorStein, Janet L.
dc.date2022-08-11T08:09:00.000
dc.date.accessioned2022-08-23T16:14:59Z
dc.date.available2022-08-23T16:14:59Z
dc.date.issued1999-02-18
dc.date.submitted2008-10-15
dc.identifier.citation<p>J Cell Biochem. 1999 Mar 15;72(4):507-16.</p>
dc.identifier.issn0730-2312 (Print)
dc.identifier.doi10.1002/(SICI)1097-4644(19990315)72:4<507::AID-JCB6>3.0.CO;2-5
dc.identifier.pmid10022610
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33991
dc.description.abstractMultiple regulatory elements and intricate protein-DNA interactions mediate the transcription of the human histone H4 genes in a cell growth-dependent manner. Upon analysis of the regulatory elements of the FO108 histone H4 gene, we identified several potential YY1 binding sites. In this study, we have analyzed the ability of the transcription factor YY1 to interact at these sites in vitro by using electrophoretic mobility shift assays in combination with oligonucleotide competition and antibody immunoreactivity. We show that YY1 specifically binds transcriptional regulatory elements at -340 nt (site III), -100 nt (site I) and at least two domains within the coding region of the histone H4 gene. To test if these elements were functionally responsive to YY1, we performed transient expression experiments in Drosophila S-2 cells transfected with heterologous reporter gene constructs driven by histone H4 gene segments fused to the thymidine kinase promoter. Co-expression of YY1 stimulated promoter activity of these constructs relative to the reporter construct lacking histone H4 gene fragments. Our results suggest that YY1 contributes to transcriptional regulation of the histone H4 gene through interactions at multiple regulatory elements.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10022610&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1002/(SICI)1097-4644(19990315)72:4<507::AID-JCB6>3.0.CO;2-5
dc.subjectAnimals; Binding Sites; Cell Line; DNA-Binding Proteins; Drosophila; Erythroid-Specific DNA-Binding Factors; Gene Expression Regulation; Genes, Reporter; Histones; Humans; Oligodeoxyribonucleotides; Promoter Regions (Genetics); Regulatory Sequences, Nucleic Acid; Transcription Factors; Transfection; YY1 Transcription Factor
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleMultiple interactions of the transcription factor YY1 with human histone H4 gene regulatory elements
dc.typeJournal Article
dc.source.journaltitleJournal of cellular biochemistry
dc.source.volume72
dc.source.issue4
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/644
dc.identifier.contextkey651114
html.description.abstract<p>Multiple regulatory elements and intricate protein-DNA interactions mediate the transcription of the human histone H4 genes in a cell growth-dependent manner. Upon analysis of the regulatory elements of the FO108 histone H4 gene, we identified several potential YY1 binding sites. In this study, we have analyzed the ability of the transcription factor YY1 to interact at these sites in vitro by using electrophoretic mobility shift assays in combination with oligonucleotide competition and antibody immunoreactivity. We show that YY1 specifically binds transcriptional regulatory elements at -340 nt (site III), -100 nt (site I) and at least two domains within the coding region of the histone H4 gene. To test if these elements were functionally responsive to YY1, we performed transient expression experiments in Drosophila S-2 cells transfected with heterologous reporter gene constructs driven by histone H4 gene segments fused to the thymidine kinase promoter. Co-expression of YY1 stimulated promoter activity of these constructs relative to the reporter construct lacking histone H4 gene fragments. Our results suggest that YY1 contributes to transcriptional regulation of the histone H4 gene through interactions at multiple regulatory elements.</p>
dc.identifier.submissionpathgsbs_sp/644
dc.contributor.departmentDepartment of Cell Biology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages507-16


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