Analysis of a novel HDAC8-H1.3 complex in several human carcinoma cell lines

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dc.contributor.authorGonzalez, Rhiannon
dc.contributor.committeeChairBergel, Michael
dc.contributor.committeeMemberConrad-Webb, Heather
dc.contributor.committeeMemberMills, Nathaniel
dc.contributor.committeeMemberMaier, Camelia
dc.contributor.committeeMemberVijayagopal, Parakat
dc.date.accessioned2017-12-13T19:29:11Z
dc.date.available2017-12-13T19:29:11Z
dc.date.issued5/30/2016
dc.description.abstractThe compaction level of chromatin regulates DNA accessibility, gene expression, and cell division. Transcription factors and other proteins cannot access the DNA within compacted chromatin. Two types of proteins that contribute to chromatin compaction are histone deacetylases (HDACs) and linker histones (H1s). H1s are chromatin-binding structural proteins required for the formation of the higher order chromatin structure. H1 subtypes also differentially regulate transcription and apoptosis. HDACs cause chromatin compaction by deacetylating lysine residues on core histone tails, causing core histones to closely interact with DNA. HDACs regulate many other cellular processes including: mitosis, intracellular trafficking, microtubule dynamics, and cell cycle events, through deacetylation of non-histone proteins. This work describes a novel HDAC8-H1.3 protein complex found in several human cancerous cell lines. The goal of this research was to gather insight as to the function of the HDAC8-H1.3 complex using co-immunoprecipitation, chromatin-binding electrophoretic mobility shift assays, deacetylation assays, immunocytochemistry, confocal microscopy, and complex protein mixture identification by LC/MS/MS. The hypothesis was that HDAC8 and H1.3 work synergistically to cause chromatin compaction. Results showed that H1.3, but not HDAC8 binds to nucleosomes. HDAC8 was found to deacetylate H1.3. In MCF-7 cells the complex was found to associate with ER-Golgi associated vesicles and late endosomes during interphase. This is the first report for a non-mitotic cytoplasmic association of a linker histone and HDAC. Also, this is the first reported association of a linker histone with vesicle trafficking.en_US
dc.identifier.urihttp://hdl.handle.net/11274/8927
dc.language.isoen_USen_US
dc.subjectBiological sciencesen_US
dc.subjectHealth and environmental sciencesen_US
dc.subjectCarcinomaen_US
dc.subjectH1en_US
dc.subjectHDACen_US
dc.subjectHistone deacetylasesen_US
dc.subjectLinker histoneen_US
dc.subjectMCF-7en_US
dc.titleAnalysis of a novel HDAC8-H1.3 complex in several human carcinoma cell linesen_US
dc.typeThesisen_US
thesis.degree.collegeCollege of Arts and Sciences
thesis.degree.departmentBiology
thesis.degree.disciplineMolecular Biology
thesis.degree.grantorTexas Woman's University
thesis.degree.levelDoctoral
thesis.degree.nameDoctor of Philosophy

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