{"id":{"repo_id":"cape-town","oai_identifier":"oai:open.uct.ac.za:11427/4342"},"canonical_url":"https://search.dev.ndltd.org/etd/cape-town/oai:open.uct.ac.za:11427/4342","repository":{"repo_id":"cape-town","name":"University of Cape Town","base_url":"https://open.uct.ac.za/oai/request"},"display":{"title":"Investigating the role of a yeast membrane protein, HSP30 in tolerance to ethanol stress","abstract":"One of the contributors of the widespread interest the yeast Saccharomyces cerevisiae has received is its ability to yield and tolerate high levels of ethanol. S. cerevisiae is able to grow and remain viable in growth media containing ethanol concentrations as high as 19.8% (w/v), a level that is toxic to many other microorganisms. Since production of ethanol is a normal event in the growth cycyle of S. cerevisiae, this organisms has evolved a number of mechanisms to cope with deleterious effects of ethanol. These include induction of heat shock proteins (HSPs). Among these, HSP30 is particularly interesting in that it is the only stress-induced protein known to be instrinsically bound to the yeast plasma membrane. Another ethanol induced HSP; HSP12 has previously been shown to have a peripheral plasma membrane localisation. It has further been shown that HSP12 protects liposomes against damage by ethanol. This study was initially aimed at investigating whether there is co-operation between HSP30 and HSP12 in this membrane protection role.","abstract_html":"One of the contributors of the widespread interest the yeast Saccharomyces cerevisiae has received is its ability to yield and tolerate high levels of ethanol. S. cerevisiae is able to grow and remain viable in growth media containing ethanol concentrations as high as 19.8% (w/v), a level that is toxic to many other microorganisms. Since production of ethanol is a normal event in the growth cycyle of S. cerevisiae, this organisms has evolved a number of mechanisms to cope with deleterious effects of ethanol. These include induction of heat shock proteins (HSPs). Among these, HSP30 is particularly interesting in that it is the only stress-induced protein known to be instrinsically bound to the yeast plasma membrane. Another ethanol induced HSP; HSP12 has previously been shown to have a peripheral plasma membrane localisation. It has further been shown that HSP12 protects liposomes against damage by ethanol. This study was initially aimed at investigating whether there is co-operation between HSP30 and HSP12 in this membrane protection role.","abstract_has_math":false,"creators":["Tsekoa, Tsepo"],"institution":"Department of Molecular and Cell Biology","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Lindsey, George G","Brandt, Wolf F"],"committee_chairs":[],"committee_members":[],"year":2001,"date_issued":"2001","date_published":"2001","updated_at":"2026-07-22T22:23:09Z","subjects":[],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/11427/4342","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Lindsey, George G","Brandt, Wolf F"]},{"key":"dc:creator","label":"Author","values":["Tsekoa, Tsepo"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2014-07-30T17:42:11Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2014-07-30T17:42:11Z"]},{"key":"dc:date.issued","label":"Date","values":["2001"]},{"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/11427/4342"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Bibliography: leaves 59-64."]},{"key":"dc:description.abstract","label":"Abstract","values":["One of the contributors of the widespread interest the yeast Saccharomyces cerevisiae has received is its ability to yield and tolerate high levels of ethanol. S. cerevisiae is able to grow and remain viable in growth media containing ethanol concentrations as high as 19.8% (w/v), a level that is toxic to many other microorganisms. Since production of ethanol is a normal event in the growth cycyle of S. cerevisiae, this organisms has evolved a number of mechanisms to cope with deleterious effects of ethanol. These include induction of heat shock proteins (HSPs). Among these, HSP30 is particularly interesting in that it is the only stress-induced protein known to be instrinsically bound to the yeast plasma membrane. Another ethanol induced HSP; HSP12 has previously been shown to have a peripheral plasma membrane localisation. It has further been shown that HSP12 protects liposomes against damage by ethanol. This study was initially aimed at investigating whether there is co-operation between HSP30 and HSP12 in this membrane protection role."]},{"key":"dc:title","label":"Title","values":["Investigating the role of a yeast membrane protein, HSP30 in tolerance to ethanol stress"]}]}],"canonical_facts":{"dc:contributor.advisor":["Lindsey, George G","Brandt, Wolf F"],"dc:creator":["Tsekoa, Tsepo"],"dc:date.accessioned":["2014-07-30T17:42:11Z"],"dc:date.available":["2014-07-30T17:42:11Z"],"dc:date.issued":["2001"],"dc:description":["Bibliography: leaves 59-64."],"dc:description.abstract":["One of the contributors of the widespread interest the yeast Saccharomyces cerevisiae has received is its ability to yield and tolerate high levels of ethanol. S. cerevisiae is able to grow and remain viable in growth media containing ethanol concentrations as high as 19.8% (w/v), a level that is toxic to many other microorganisms. Since production of ethanol is a normal event in the growth cycyle of S. cerevisiae, this organisms has evolved a number of mechanisms to cope with deleterious effects of ethanol. These include induction of heat shock proteins (HSPs). Among these, HSP30 is particularly interesting in that it is the only stress-induced protein known to be instrinsically bound to the yeast plasma membrane. Another ethanol induced HSP; HSP12 has previously been shown to have a peripheral plasma membrane localisation. It has further been shown that HSP12 protects liposomes against damage by ethanol. This study was initially aimed at investigating whether there is co-operation between HSP30 and HSP12 in this membrane protection role."],"dc:identifier.uri":["http://hdl.handle.net/11427/4342"],"dc:language.iso":["eng"],"dc:publisher.department":["Department of Molecular and Cell Biology"],"dc:publisher.institution":["University of Cape Town"],"dc:title":["Investigating the role of a yeast membrane protein, HSP30 in tolerance to ethanol stress"],"dc:type":["Master Thesis"],"dc:type.qualificationlevel":["Masters"],"dc:type.qualificationname":["MSc"]},"updated_at":"2026-07-22T22:23:09Z"}