{"id":{"repo_id":"cape-town","oai_identifier":"oai:open.uct.ac.za:11427/4335"},"canonical_url":"https://search.dev.ndltd.org/etd/cape-town/oai:open.uct.ac.za:11427/4335","repository":{"repo_id":"cape-town","name":"University of Cape Town","base_url":"https://open.uct.ac.za/oai/request"},"display":{"title":"The phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phase","abstract":"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.","abstract_html":"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.","abstract_has_math":false,"creators":["Somers, Sachin J"],"institution":"Department of Molecular and Cell Biology","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Patterton, Hugh"],"committee_chairs":[],"committee_members":[],"year":2005,"date_issued":"2005","date_published":"2005","updated_at":"2026-07-22T22:22:50Z","subjects":[],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/11427/4335","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Patterton, Hugh"]},{"key":"dc:creator","label":"Author","values":["Somers, Sachin J"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2014-07-30T17:41:58Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2014-07-30T17:41:58Z"]},{"key":"dc:date.issued","label":"Date","values":["2005"]},{"key":"dc:publisher.department","label":"Dc Publisher Department","values":["Department of Molecular and Cell Biology"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["University of Cape Town"]},{"key":"dc:type","label":"Dc Type","values":["Master Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["Masters"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["MSc"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/11427/4335"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Includes bibliographical references."]},{"key":"dc:description.abstract","label":"Abstract","values":["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."]},{"key":"dc:title","label":"Title","values":["The phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phase"]}]}],"canonical_facts":{"dc:contributor.advisor":["Patterton, Hugh"],"dc:creator":["Somers, Sachin J"],"dc:date.accessioned":["2014-07-30T17:41:58Z"],"dc:date.available":["2014-07-30T17:41:58Z"],"dc:date.issued":["2005"],"dc:description":["Includes bibliographical references."],"dc:description.abstract":["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."],"dc:identifier.uri":["http://hdl.handle.net/11427/4335"],"dc:language.iso":["eng"],"dc:publisher.department":["Department of Molecular and Cell Biology"],"dc:publisher.institution":["University of Cape Town"],"dc:title":["The phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phase"],"dc:type":["Master Thesis"],"dc:type.qualificationlevel":["Masters"],"dc:type.qualificationname":["MSc"]},"updated_at":"2026-07-22T22:22:50Z"}