The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress.
dc.contributor.author | Sales, Kurt | |
dc.contributor.author | Brandt, Wolf | |
dc.contributor.author | Rumbak, Elaine | |
dc.contributor.author | Lindsey, George | |
dc.date.accessioned | 2016-08-02T09:42:23Z | |
dc.date.available | 2016-08-02T09:42:23Z | |
dc.date.issued | 2000 | |
dc.date.updated | 2016-08-02T07:50:10Z | |
dc.description.abstract | The LEA-like protein HSP 12 was identified as having a plasma membrane location in yeast. Gold particles, indicative of the presence of HSP 12, were observed on the external side of the plasma membrane when yeast grown to stationary phase were subjected to immunocytochemical analysis. Growth of yeast in the osmolyte mannitol resulted in an increased number of gold particles that were now observed to be present on both sides of the plasma membrane. No gold particles were observed using a mutant strain of the same yeast that did not express HSP 12. A model liposome system encapsulating the fluorescent dye calcein was used to investigate the protection by HSP 12 of membranes during desiccation. HSP 12 was found to act in an analogous manner to trehalose and protect liposomal membrane integrity against desiccation. The interaction between HSP 12 and the liposomal membrane was judged to be electrostatic as membrane protection was only observed with positively charged liposomes and not with either neutral or negatively charged liposomes. The ability of the wild-type and mutant yeast to grow in media containing ethanol was compared. It was found that yeast not expressing the HSP 12 protein were less able to grow in media containing ethanol. HSP 12 was shown to confer increased integrity on the liposomal membrane in the presence of ethanol. Ethanol, like mannitol, was found to induce HSP 12 protein synthesis. However, yeast grown in both ethanol and mannitol showed a decreased HSP 12 response compared with yeast grown in the presence of either osmolyte alone. | en_ZA |
dc.identifier | http://dx.doi.org/10.1016/S0005-2736(99)00215-1 | |
dc.identifier.apacitation | Sales, K., Brandt, W., Rumbak, E., & Lindsey, G. (2000). The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress. <i>Biochimica et Biophysica Acta</i>, http://hdl.handle.net/11427/21096 | en_ZA |
dc.identifier.chicagocitation | Sales, Kurt, Wolf Brandt, Elaine Rumbak, and George Lindsey "The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress." <i>Biochimica et Biophysica Acta</i> (2000) http://hdl.handle.net/11427/21096 | en_ZA |
dc.identifier.citation | Sales, K., Brandt, W., Rumbak, E., & Lindsey, G. (2000). The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1463(2), 267-278. | en_ZA |
dc.identifier.issn | 0006-3002 | en_ZA |
dc.identifier.ris | TY - Journal Article AU - Sales, Kurt AU - Brandt, Wolf AU - Rumbak, Elaine AU - Lindsey, George AB - The LEA-like protein HSP 12 was identified as having a plasma membrane location in yeast. Gold particles, indicative of the presence of HSP 12, were observed on the external side of the plasma membrane when yeast grown to stationary phase were subjected to immunocytochemical analysis. Growth of yeast in the osmolyte mannitol resulted in an increased number of gold particles that were now observed to be present on both sides of the plasma membrane. No gold particles were observed using a mutant strain of the same yeast that did not express HSP 12. A model liposome system encapsulating the fluorescent dye calcein was used to investigate the protection by HSP 12 of membranes during desiccation. HSP 12 was found to act in an analogous manner to trehalose and protect liposomal membrane integrity against desiccation. The interaction between HSP 12 and the liposomal membrane was judged to be electrostatic as membrane protection was only observed with positively charged liposomes and not with either neutral or negatively charged liposomes. The ability of the wild-type and mutant yeast to grow in media containing ethanol was compared. It was found that yeast not expressing the HSP 12 protein were less able to grow in media containing ethanol. HSP 12 was shown to confer increased integrity on the liposomal membrane in the presence of ethanol. Ethanol, like mannitol, was found to induce HSP 12 protein synthesis. However, yeast grown in both ethanol and mannitol showed a decreased HSP 12 response compared with yeast grown in the presence of either osmolyte alone. DA - 2000 DB - OpenUCT DP - University of Cape Town J1 - Biochimica et Biophysica Acta LK - https://open.uct.ac.za PB - University of Cape Town PY - 2000 SM - 0006-3002 T1 - The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress TI - The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress UR - http://hdl.handle.net/11427/21096 ER - | en_ZA |
dc.identifier.uri | http://hdl.handle.net/11427/21096 | |
dc.identifier.vancouvercitation | Sales K, Brandt W, Rumbak E, Lindsey G. The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress. Biochimica et Biophysica Acta. 2000; http://hdl.handle.net/11427/21096. | en_ZA |
dc.language | eng | en_ZA |
dc.publisher | Elsevier | en_ZA |
dc.publisher.institution | University of Cape Town | |
dc.rights | Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | en_ZA |
dc.source | Biochimica et Biophysica Acta | en_ZA |
dc.source.uri | https://www.elsevier.com/journals/bba-biochimica-et-biophysica-acta/fs00-0253 | |
dc.subject.other | Liposomes | |
dc.subject.other | Ethanol | |
dc.subject.other | LEA proteins | |
dc.subject.other | Desiccation | |
dc.title | The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress. | en_ZA |
dc.type | Journal Article | en_ZA |
uct.type.filetype | Text | |
uct.type.filetype | Image | |
uct.type.publication | Research | en_ZA |
uct.type.resource | Article | en_ZA |