The phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phase

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dc.contributor.advisorPatterton, Hughen_ZA
dc.contributor.authorSomers, Sachin Jen_ZA
dc.date.accessioned2014-07-30T17:41:58Z
dc.date.available2014-07-30T17:41:58Z
dc.date.issued2005en_ZA
dc.descriptionIncludes bibliographical references.
dc.description.abstractOur group has recently found that the linker histone Hh01 p of Saccharomyces cerevisiae exhibited a significant increase in binding to chromatin during stationary phase. Because of the role of H1 in gene expression and chromatin compaction, it is essential to understand the mechanism behind this change in binding behaviour for a complete mechanistic description of gene regulation. We postulated that the phosphorylation of serine or threonine residues decrease the affinity of H1 for DNA, resulting in the dissociation of H1 from chromatin in exponential phase. We investigated this possible change in the phosphorylation state of Hh01 p in yeast cells in exponential phase and in stationary phase by immunoprecipitation of Hh01 p, followed by western analysis using antiphosphoserine and anti-phosphothreonine antibodies.en_ZA
dc.identifier.apacitationSomers, S. J. (2005). <i>The phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phase</i>. (Thesis). University of Cape Town ,Faculty of Science ,Department of Molecular and Cell Biology. Retrieved from http://hdl.handle.net/11427/4335en_ZA
dc.identifier.chicagocitationSomers, Sachin J. <i>"The phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phase."</i> Thesis., University of Cape Town ,Faculty of Science ,Department of Molecular and Cell Biology, 2005. http://hdl.handle.net/11427/4335en_ZA
dc.identifier.citationSomers, S. 2005. The phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phase. University of Cape Town.en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - Somers, Sachin J AB - Our group has recently found that the linker histone Hh01 p of Saccharomyces cerevisiae exhibited a significant increase in binding to chromatin during stationary phase. Because of the role of H1 in gene expression and chromatin compaction, it is essential to understand the mechanism behind this change in binding behaviour for a complete mechanistic description of gene regulation. We postulated that the phosphorylation of serine or threonine residues decrease the affinity of H1 for DNA, resulting in the dissociation of H1 from chromatin in exponential phase. We investigated this possible change in the phosphorylation state of Hh01 p in yeast cells in exponential phase and in stationary phase by immunoprecipitation of Hh01 p, followed by western analysis using antiphosphoserine and anti-phosphothreonine antibodies. DA - 2005 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 2005 T1 - The phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phase TI - The phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phase UR - http://hdl.handle.net/11427/4335 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/4335
dc.identifier.vancouvercitationSomers SJ. The phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phase. [Thesis]. University of Cape Town ,Faculty of Science ,Department of Molecular and Cell Biology, 2005 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/4335en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDepartment of Molecular and Cell Biologyen_ZA
dc.publisher.facultyFaculty of Scienceen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.subject.otherCell Biologyen_ZA
dc.titleThe phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phaseen_ZA
dc.typeMaster Thesis
dc.type.qualificationlevelMasters
dc.type.qualificationnameMScen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceThesisen_ZA
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