Protein/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.contributor.author | Van Wijnen, Andre J. | |
dc.contributor.author | Lian, Jane B. | |
dc.contributor.author | Stein, Janet L. | |
dc.contributor.author | Stein, Gary S. | |
dc.date | 2022-08-11T08:08:50.000 | |
dc.date.accessioned | 2022-08-23T16:09:35Z | |
dc.date.available | 2022-08-23T16:09:35Z | |
dc.date.issued | 1991-12-01 | |
dc.date.submitted | 2009-01-13 | |
dc.identifier.citation | J 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.issn | 0730-2312 (Print) | |
dc.identifier.doi | 10.1002/jcb.240470408 | |
dc.identifier.pmid | 1795016 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/32732 | |
dc.description.abstract | 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. | |
dc.language.iso | en_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.url | http://dx.doi.org/10.1002/jcb.240470408 | |
dc.subject | Activating 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.subject | Life Sciences | |
dc.subject | Medicine and Health Sciences | |
dc.title | Protein/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.type | Journal Article | |
dc.source.journaltitle | Journal of cellular biochemistry | |
dc.source.volume | 47 | |
dc.source.issue | 4 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/gsbs_sp/1288 | |
dc.identifier.contextkey | 693217 | |
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.submissionpath | gsbs_sp/1288 | |
dc.contributor.department | Department of Cell Biology | |
dc.contributor.department | Graduate School of Biomedical Sciences | |
dc.source.pages | 337-51 |