Mammalian Bax triggers apoptotic changes in yeast
Apoptosis is co-regulated by the conserved family of Bcl-2-related proteins, which includes both its agonists (Bax) and antagonists (Bcl-X L). A mutant strain of the yeast Saccharomyces cerevisiae has been shown to express all morphological signs of apoptosis. Overexpression of Bax is lethal in S. c...
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| Veröffentlicht in: | FEBS letters 1998-10, Vol.438 (1), p.61-65 |
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| container_title | FEBS letters |
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| creator | Ligr, Martin Madeo, Frank Fröhlich, Eleonore Hilt, Wolfgang Fröhlich, Kai-Uwe Wolf, Dieter H |
| description | Apoptosis is co-regulated by the conserved family of Bcl-2-related proteins, which includes both its agonists (Bax) and antagonists (Bcl-X
L). A mutant strain of the yeast
Saccharomyces cerevisiae has been shown to express all morphological signs of apoptosis. Overexpression of Bax is lethal in
S. cerevisiae, whereas simultaneous overexpression of Bcl-X
L rescues the cells. We report that overexpression of mammalian Bax in a
S. cerevisiae wild type strain triggers morphological changes similar to those of apoptotic metazoan cells: the loss of asymmetric distribution of plasma membrane phosphatidylserine, plasma membrane blebbing, chromatin condensation and margination, and DNA fragmentation. Simultaneous overexpression of Bcl-X
L prevents these changes. We demonstrate that Bax triggers phenotypic alterations in yeast strongly resembling those it causes in metazoan apoptotic cells. |
| doi_str_mv | 10.1016/S0014-5793(98)01227-7 |
| format | Article |
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L). A mutant strain of the yeast
Saccharomyces cerevisiae has been shown to express all morphological signs of apoptosis. Overexpression of Bax is lethal in
S. cerevisiae, whereas simultaneous overexpression of Bcl-X
L rescues the cells. We report that overexpression of mammalian Bax in a
S. cerevisiae wild type strain triggers morphological changes similar to those of apoptotic metazoan cells: the loss of asymmetric distribution of plasma membrane phosphatidylserine, plasma membrane blebbing, chromatin condensation and margination, and DNA fragmentation. Simultaneous overexpression of Bcl-X
L prevents these changes. We demonstrate that Bax triggers phenotypic alterations in yeast strongly resembling those it causes in metazoan apoptotic cells.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(98)01227-7</identifier><identifier>PMID: 9821959</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Apoptosis ; Bax ; bcl-2-Associated X Protein ; bcl-X Protein ; Cell Membrane - metabolism ; Cell Membrane - ultrastructure ; Cell Nucleus - metabolism ; Cell Nucleus - ultrastructure ; Chromatin - metabolism ; DAPI, diaminophenylindole ; DNA Fragmentation ; Gene Transfer Techniques ; In Situ Nick-End Labeling ; Indoles ; Mammals - genetics ; Microscopy, Electron ; Phosphatidylserines - metabolism ; PI, propidium iodide ; Proto-Oncogene Proteins - genetics ; Proto-Oncogene Proteins - physiology ; Proto-Oncogene Proteins c-bcl-2 - genetics ; Proto-Oncogene Proteins c-bcl-2 - physiology ; PS, phosphatidylserine ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; SC, synthetic complete growth medium ; TUNEL, terminal deoxynucleotidyl transferase-mediated dUTP nick end-labeling ; Yeast Saccharomyces cerevisiae</subject><ispartof>FEBS letters, 1998-10, Vol.438 (1), p.61-65</ispartof><rights>1998 Federation of European Biochemical Societies</rights><rights>FEBS Letters 438 (1998) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5387-a5775ae8efd4f3e3a095d47a2521d100faae2bf11ac26d8fbc6559f6ac284ed13</citedby><cites>FETCH-LOGICAL-c5387-a5775ae8efd4f3e3a095d47a2521d100faae2bf11ac26d8fbc6559f6ac284ed13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2898%2901227-7$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(98)01227-7$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9821959$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ligr, Martin</creatorcontrib><creatorcontrib>Madeo, Frank</creatorcontrib><creatorcontrib>Fröhlich, Eleonore</creatorcontrib><creatorcontrib>Hilt, Wolfgang</creatorcontrib><creatorcontrib>Fröhlich, Kai-Uwe</creatorcontrib><creatorcontrib>Wolf, Dieter H</creatorcontrib><title>Mammalian Bax triggers apoptotic changes in yeast</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Apoptosis is co-regulated by the conserved family of Bcl-2-related proteins, which includes both its agonists (Bax) and antagonists (Bcl-X
L). A mutant strain of the yeast
Saccharomyces cerevisiae has been shown to express all morphological signs of apoptosis. Overexpression of Bax is lethal in
S. cerevisiae, whereas simultaneous overexpression of Bcl-X
L rescues the cells. We report that overexpression of mammalian Bax in a
S. cerevisiae wild type strain triggers morphological changes similar to those of apoptotic metazoan cells: the loss of asymmetric distribution of plasma membrane phosphatidylserine, plasma membrane blebbing, chromatin condensation and margination, and DNA fragmentation. Simultaneous overexpression of Bcl-X
L prevents these changes. We demonstrate that Bax triggers phenotypic alterations in yeast strongly resembling those it causes in metazoan apoptotic cells.</description><subject>Animals</subject><subject>Apoptosis</subject><subject>Bax</subject><subject>bcl-2-Associated X Protein</subject><subject>bcl-X Protein</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Membrane - ultrastructure</subject><subject>Cell Nucleus - metabolism</subject><subject>Cell Nucleus - ultrastructure</subject><subject>Chromatin - metabolism</subject><subject>DAPI, diaminophenylindole</subject><subject>DNA Fragmentation</subject><subject>Gene Transfer Techniques</subject><subject>In Situ Nick-End Labeling</subject><subject>Indoles</subject><subject>Mammals - genetics</subject><subject>Microscopy, Electron</subject><subject>Phosphatidylserines - metabolism</subject><subject>PI, propidium iodide</subject><subject>Proto-Oncogene Proteins - genetics</subject><subject>Proto-Oncogene Proteins - physiology</subject><subject>Proto-Oncogene Proteins c-bcl-2 - genetics</subject><subject>Proto-Oncogene Proteins c-bcl-2 - physiology</subject><subject>PS, phosphatidylserine</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>SC, synthetic complete growth medium</subject><subject>TUNEL, terminal deoxynucleotidyl transferase-mediated dUTP nick end-labeling</subject><subject>Yeast Saccharomyces cerevisiae</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE9PwzAMxSMEGmPwESb1hOBQSNqmSU6ITRtDGuIAnCMvdUdQ_4ykA_btabdpVzhZ9nt-tn6EDBm9YZSlty-UsiTkQsVXSl5TFkUiFEekz6SIwzhJ5THpHyyn5Mz7D9r2kqke6SkZMcVVn7AnKEsoLFTBCH6CxtnlEp0PYFWvmrqxJjDvUC3RB7YKNgi-OScnORQeL_Z1QN6mk9fxLJw_PzyO7-eh4bEUIXAhOKDEPEvyGGOgimeJgIhHLGOU5gAYLXLGwERpJvOFSTlXedq2MsGMxQNyuctdufpzjb7RpfUGiwIqrNdeC0q5VHFn5DujcbX3DnO9crYEt9GM6g6V3qLSHQetpN6i0qLdG-4PrBclZoetPZtWn-30b1vg5n-hejoZRVulE5TcjrtTd7sobIF9WXTaG4uVwcw6NI3OavvHs7_Wn4wj</recordid><startdate>19981030</startdate><enddate>19981030</enddate><creator>Ligr, Martin</creator><creator>Madeo, Frank</creator><creator>Fröhlich, Eleonore</creator><creator>Hilt, Wolfgang</creator><creator>Fröhlich, Kai-Uwe</creator><creator>Wolf, Dieter H</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19981030</creationdate><title>Mammalian Bax triggers apoptotic changes in yeast</title><author>Ligr, Martin ; Madeo, Frank ; Fröhlich, Eleonore ; Hilt, Wolfgang ; Fröhlich, Kai-Uwe ; Wolf, Dieter H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5387-a5775ae8efd4f3e3a095d47a2521d100faae2bf11ac26d8fbc6559f6ac284ed13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Apoptosis</topic><topic>Bax</topic><topic>bcl-2-Associated X Protein</topic><topic>bcl-X Protein</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Membrane - ultrastructure</topic><topic>Cell Nucleus - metabolism</topic><topic>Cell Nucleus - ultrastructure</topic><topic>Chromatin - metabolism</topic><topic>DAPI, diaminophenylindole</topic><topic>DNA Fragmentation</topic><topic>Gene Transfer Techniques</topic><topic>In Situ Nick-End Labeling</topic><topic>Indoles</topic><topic>Mammals - genetics</topic><topic>Microscopy, Electron</topic><topic>Phosphatidylserines - metabolism</topic><topic>PI, propidium iodide</topic><topic>Proto-Oncogene Proteins - genetics</topic><topic>Proto-Oncogene Proteins - physiology</topic><topic>Proto-Oncogene Proteins c-bcl-2 - genetics</topic><topic>Proto-Oncogene Proteins c-bcl-2 - physiology</topic><topic>PS, phosphatidylserine</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>SC, synthetic complete growth medium</topic><topic>TUNEL, terminal deoxynucleotidyl transferase-mediated dUTP nick end-labeling</topic><topic>Yeast Saccharomyces cerevisiae</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ligr, Martin</creatorcontrib><creatorcontrib>Madeo, Frank</creatorcontrib><creatorcontrib>Fröhlich, Eleonore</creatorcontrib><creatorcontrib>Hilt, Wolfgang</creatorcontrib><creatorcontrib>Fröhlich, Kai-Uwe</creatorcontrib><creatorcontrib>Wolf, Dieter H</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ligr, Martin</au><au>Madeo, Frank</au><au>Fröhlich, Eleonore</au><au>Hilt, Wolfgang</au><au>Fröhlich, Kai-Uwe</au><au>Wolf, Dieter H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mammalian Bax triggers apoptotic changes in yeast</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1998-10-30</date><risdate>1998</risdate><volume>438</volume><issue>1</issue><spage>61</spage><epage>65</epage><pages>61-65</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Apoptosis is co-regulated by the conserved family of Bcl-2-related proteins, which includes both its agonists (Bax) and antagonists (Bcl-X
L). A mutant strain of the yeast
Saccharomyces cerevisiae has been shown to express all morphological signs of apoptosis. Overexpression of Bax is lethal in
S. cerevisiae, whereas simultaneous overexpression of Bcl-X
L rescues the cells. We report that overexpression of mammalian Bax in a
S. cerevisiae wild type strain triggers morphological changes similar to those of apoptotic metazoan cells: the loss of asymmetric distribution of plasma membrane phosphatidylserine, plasma membrane blebbing, chromatin condensation and margination, and DNA fragmentation. Simultaneous overexpression of Bcl-X
L prevents these changes. We demonstrate that Bax triggers phenotypic alterations in yeast strongly resembling those it causes in metazoan apoptotic cells.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9821959</pmid><doi>10.1016/S0014-5793(98)01227-7</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1998-10, Vol.438 (1), p.61-65 |
| issn | 0014-5793 1873-3468 |
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| source | MEDLINE; Access via Wiley Online Library; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection); Alma/SFX Local Collection |
| subjects | Animals Apoptosis Bax bcl-2-Associated X Protein bcl-X Protein Cell Membrane - metabolism Cell Membrane - ultrastructure Cell Nucleus - metabolism Cell Nucleus - ultrastructure Chromatin - metabolism DAPI, diaminophenylindole DNA Fragmentation Gene Transfer Techniques In Situ Nick-End Labeling Indoles Mammals - genetics Microscopy, Electron Phosphatidylserines - metabolism PI, propidium iodide Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins - physiology Proto-Oncogene Proteins c-bcl-2 - genetics Proto-Oncogene Proteins c-bcl-2 - physiology PS, phosphatidylserine Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism SC, synthetic complete growth medium TUNEL, terminal deoxynucleotidyl transferase-mediated dUTP nick end-labeling Yeast Saccharomyces cerevisiae |
| title | Mammalian Bax triggers apoptotic changes in yeast |
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