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dc.contributor.authorMiele, Angela
dc.contributor.authorMedina, Ricardo F.
dc.contributor.authorVan Wijnen, Andre J.
dc.contributor.authorStein, Gary S.
dc.contributor.authorStein, Janet L.
dc.date2022-08-11T08:08:58.000
dc.date.accessioned2022-08-23T16:14:04Z
dc.date.available2022-08-23T16:14:04Z
dc.date.issued2007-06-20
dc.date.submitted2008-09-22
dc.identifier.citationJ Cell Biochem. 2007 Sep 1;102(1):136-48. <a href="http://dx.doi.org/10.1002/jcb.21284">Link to article on publisher's site</a>
dc.identifier.issn0730-2312 (Print)
dc.identifier.doi10.1002/jcb.21284
dc.identifier.pmid17577209
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33775
dc.description.abstractHiNF-P is a recently identified histone H4 subtype specific transcriptional regulator that associates with the conserved cell cycle control element in the proximal promoter regions of histone H4 genes. HiNF-P interacts with the global histone gene regulator and direct cyclin E/CDK2 substrate p220(NPAT) to potently upregulate histone H4 gene transcription at the G1/S phase transition in response to cyclin E/CDK2 signaling. To gain insight into the function of HiNF-P in a broader cellular context, we performed a yeast two-hybrid screen to identify its novel interacting proteins. In this study, we detected 67 candidate HiNF-P interacting proteins of varying cellular functions. We have identified multiple RNA associated proteins, including the splicing co-factor SRm300. HiNF-P and SRm300 interact in yeast two-hybrid, co-immunoprecipitation, and co-immunofluorescence assays. Our screen also identified several gene regulators that associate with HiNF-P including THAP7. HiNF-P and THAP7 interact in mammalian cells and THAP7 abrogates HiNF-P/p220 mediated activation of histone H4 gene transcription, consistent with its known role as a transcriptional repressor. Finally, we identified several proliferation related proteins including Ki-67 and X transactivated protein 2 (XTP2) which may be functioning with HiNF-P in cell cycle regulation. The HiNF-P interactome indicates that HiNF-P is a multifunctional gene regulator with a large functional network and roles beyond cell cycle-dependent histone gene regulation.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=17577209&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1002/jcb.21284
dc.subjectCell Cycle; Cell Line, Tumor; Cell Proliferation; Chromosomal Proteins, Non-Histone; *Gene Expression Regulation; Humans; Ki-67 Antigen; *RNA Processing, Post-Transcriptional; RNA-Binding Proteins; Repressor Proteins; Transcription, Genetic; Two-Hybrid System Techniques
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleThe interactome of the histone gene regulatory factor HiNF-P suggests novel cell cycle related roles in transcriptional control and RNA processing
dc.typeJournal Article
dc.source.journaltitleJournal of cellular biochemistry
dc.source.volume102
dc.source.issue1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/436
dc.identifier.contextkey635311
html.description.abstract<p>HiNF-P is a recently identified histone H4 subtype specific transcriptional regulator that associates with the conserved cell cycle control element in the proximal promoter regions of histone H4 genes. HiNF-P interacts with the global histone gene regulator and direct cyclin E/CDK2 substrate p220(NPAT) to potently upregulate histone H4 gene transcription at the G1/S phase transition in response to cyclin E/CDK2 signaling. To gain insight into the function of HiNF-P in a broader cellular context, we performed a yeast two-hybrid screen to identify its novel interacting proteins. In this study, we detected 67 candidate HiNF-P interacting proteins of varying cellular functions. We have identified multiple RNA associated proteins, including the splicing co-factor SRm300. HiNF-P and SRm300 interact in yeast two-hybrid, co-immunoprecipitation, and co-immunofluorescence assays. Our screen also identified several gene regulators that associate with HiNF-P including THAP7. HiNF-P and THAP7 interact in mammalian cells and THAP7 abrogates HiNF-P/p220 mediated activation of histone H4 gene transcription, consistent with its known role as a transcriptional repressor. Finally, we identified several proliferation related proteins including Ki-67 and X transactivated protein 2 (XTP2) which may be functioning with HiNF-P in cell cycle regulation. The HiNF-P interactome indicates that HiNF-P is a multifunctional gene regulator with a large functional network and roles beyond cell cycle-dependent histone gene regulation.</p>
dc.identifier.submissionpathgsbs_sp/436
dc.contributor.departmentDepartment of Cell Biology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages136-48


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