Glutathione metabolism and dimorphism in Aureobasidium pullulans
Yeast⟷mycelium morphological transitions of Aureobasidium pullulans are influenced by numerous environmental factors. In general, changes in the glutathione (GSH) metabolism of dimorphic fungi may lead to alterations in the reduced thiol status of the cells that are hypothesised to initialise morpho...
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description | Yeast⟷mycelium morphological transitions of Aureobasidium pullulans are influenced by numerous environmental factors. In general, changes in the glutathione (GSH) metabolism of dimorphic fungi may lead to alterations in the reduced thiol status of the cells that are hypothesised to initialise morphological transitions. In accordance with this hypothesis, the specific GSH levels found in A. pullulans yeast cells were always significantly higher than those in mycelia. On the other hand, there was no significant difference between the GSH/GSSG redox status of the cells with either yeast or mycelial morphology. The cascade of events leading to morphological transitions was therefore unlikely to proceed via redox modulation of protein thiols. Although there were morphology‐dependent differences in the specific activities of some GSH metabolic enzymes, e.g. glutathione reductase (GR),γ‐glutamyltranspeptidase (γGT), glucose‐6‐phosphate dehydrogenase (G6PD), they were not satisfactory to explain the observed alterations in the intracellular GSH levels. It is noteworthy that very similar specific γGT and G6PD activities were found in cells separated from mixed morphology cultures independently of the actual cell morphology. On the other hand, the specific γGT and G6PD activities of A. pullulans cells sharing the same morphology but separated from pure and mixed morphology cultures showed marked differences. |
doi_str_mv | 10.1002/1521-4028(200105)41:2<131::AID-JOBM131>3.0.CO;2-# |
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In general, changes in the glutathione (GSH) metabolism of dimorphic fungi may lead to alterations in the reduced thiol status of the cells that are hypothesised to initialise morphological transitions. In accordance with this hypothesis, the specific GSH levels found in A. pullulans yeast cells were always significantly higher than those in mycelia. On the other hand, there was no significant difference between the GSH/GSSG redox status of the cells with either yeast or mycelial morphology. The cascade of events leading to morphological transitions was therefore unlikely to proceed via redox modulation of protein thiols. Although there were morphology‐dependent differences in the specific activities of some GSH metabolic enzymes, e.g. glutathione reductase (GR),γ‐glutamyltranspeptidase (γGT), glucose‐6‐phosphate dehydrogenase (G6PD), they were not satisfactory to explain the observed alterations in the intracellular GSH levels. It is noteworthy that very similar specific γGT and G6PD activities were found in cells separated from mixed morphology cultures independently of the actual cell morphology. On the other hand, the specific γGT and G6PD activities of A. pullulans cells sharing the same morphology but separated from pure and mixed morphology cultures showed marked differences.</description><identifier>ISSN: 0233-111X</identifier><identifier>EISSN: 1521-4028</identifier><identifier>DOI: 10.1002/1521-4028(200105)41:2<131::AID-JOBM131>3.0.CO;2-#</identifier><identifier>PMID: 11441460</identifier><language>eng</language><publisher>Berlin: WILEY-VCH Verlag Berlin GmbH</publisher><subject>Ascomycota - cytology ; Ascomycota - enzymology ; Ascomycota - growth & development ; Ascomycota - physiology ; Aureobasidium pullulans ; Culture Media ; g-glutamyltranspeptidase ; G6PD ; G6PD, glucose‐6‐phosphate dehydrogenase ; gGT ; gGT, g‐glutamyltranspeptidase ; glucose-6-phosphate dehydrogenase ; glutathione ; Glutathione - metabolism ; glutathione disulphide ; glutathione peroxidase ; glutathione reductase ; glutathione S-transferase ; GPx ; GPx, glutathione peroxidase ; GR, glutathione reductase ; GSH ; GSH, glutathione ; GSSG ; GSSG, glutathione disulphide ; GST ; GST, glutathione S‐transferase ; SD, standard deviation ; SOD ; SOD, superoxide dismutase ; standard deviation ; superoxide dismutase</subject><ispartof>Journal of basic microbiology, 2001-05, Vol.41 (2), p.131-137</ispartof><rights>2001 WILEY‐VCH Verlag Berlin GmbH, Fed. 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Basic Microbiol</addtitle><description>Yeast⟷mycelium morphological transitions of Aureobasidium pullulans are influenced by numerous environmental factors. In general, changes in the glutathione (GSH) metabolism of dimorphic fungi may lead to alterations in the reduced thiol status of the cells that are hypothesised to initialise morphological transitions. In accordance with this hypothesis, the specific GSH levels found in A. pullulans yeast cells were always significantly higher than those in mycelia. On the other hand, there was no significant difference between the GSH/GSSG redox status of the cells with either yeast or mycelial morphology. The cascade of events leading to morphological transitions was therefore unlikely to proceed via redox modulation of protein thiols. Although there were morphology‐dependent differences in the specific activities of some GSH metabolic enzymes, e.g. glutathione reductase (GR),γ‐glutamyltranspeptidase (γGT), glucose‐6‐phosphate dehydrogenase (G6PD), they were not satisfactory to explain the observed alterations in the intracellular GSH levels. It is noteworthy that very similar specific γGT and G6PD activities were found in cells separated from mixed morphology cultures independently of the actual cell morphology. On the other hand, the specific γGT and G6PD activities of A. pullulans cells sharing the same morphology but separated from pure and mixed morphology cultures showed marked differences.</description><subject>Ascomycota - cytology</subject><subject>Ascomycota - enzymology</subject><subject>Ascomycota - growth & development</subject><subject>Ascomycota - physiology</subject><subject>Aureobasidium pullulans</subject><subject>Culture Media</subject><subject>g-glutamyltranspeptidase</subject><subject>G6PD</subject><subject>G6PD, glucose‐6‐phosphate dehydrogenase</subject><subject>gGT</subject><subject>gGT, g‐glutamyltranspeptidase</subject><subject>glucose-6-phosphate dehydrogenase</subject><subject>glutathione</subject><subject>Glutathione - metabolism</subject><subject>glutathione disulphide</subject><subject>glutathione peroxidase</subject><subject>glutathione reductase</subject><subject>glutathione S-transferase</subject><subject>GPx</subject><subject>GPx, glutathione peroxidase</subject><subject>GR, glutathione reductase</subject><subject>GSH</subject><subject>GSH, glutathione</subject><subject>GSSG</subject><subject>GSSG, glutathione disulphide</subject><subject>GST</subject><subject>GST, glutathione S‐transferase</subject><subject>SD, standard deviation</subject><subject>SOD</subject><subject>SOD, superoxide dismutase</subject><subject>standard deviation</subject><subject>superoxide dismutase</subject><issn>0233-111X</issn><issn>1521-4028</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkN9v0zAQxy0EYqXwL6BISAgeUu5sx2nKhCgZ6zaN5YEf4-2U2o5mljQlTgT773GVMl6Qpj1Ypzt9_bnTh7EMYYYA_A0mHGMJfP6KAyAkryUu-CEKXCyWp0fxWfHhU2jeiRnM8uItj188YJPbPw_ZBLgQMSJ-P2BPvP8BAFnGs8fsAFFKlAom7P2qHvqyv3LtxkaN7ct1WzvfROXGRMY1bbe92rVuEy2Hzrbr0jvjhibaDnU91OXGP2WPqrL29tm-TtnX449f8pP4vFid5svzWEsuMS5Rp0ZCpYw2ymYwN2uVWGWyNAOlUxQKwqHa2ERJXmmhRKKtNZWdZ0kqlBZT9nLkbrv252B9T43z2tbhBtsOnlLI0rlEvDPIIQAxvCkrxqDuWu87W9G2c03Z3RAC7fzTziXtXNLonyRSmAokCv5p758EAeUF8UB8vl89rBtr_vH2ukPg8xj45Wp7c499_1v3dxCo8Uh1vre_b6lld00qFWlClxcrOrs8ObrIvwEdiz-On6u1</recordid><startdate>200105</startdate><enddate>200105</enddate><creator>Jürgensen, Claudia Würtz</creator><creator>Jacobsen, Nicklas Raun</creator><creator>Emri, Tamás</creator><creator>Havn Eriksen, Susanne</creator><creator>Pócsi, István</creator><general>WILEY-VCH Verlag Berlin GmbH</general><general>WILEY‐VCH Verlag Berlin GmbH</general><scope>BSCLL</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>M7N</scope><scope>7X8</scope></search><sort><creationdate>200105</creationdate><title>Glutathione metabolism and dimorphism in Aureobasidium pullulans</title><author>Jürgensen, Claudia Würtz ; Jacobsen, Nicklas Raun ; Emri, Tamás ; Havn Eriksen, Susanne ; Pócsi, István</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4241-a1c7d40f6dcd6e908db65e6d97906c71360111cde5642fc3635ceedfe895736c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Ascomycota - cytology</topic><topic>Ascomycota - enzymology</topic><topic>Ascomycota - growth & development</topic><topic>Ascomycota - physiology</topic><topic>Aureobasidium pullulans</topic><topic>Culture Media</topic><topic>g-glutamyltranspeptidase</topic><topic>G6PD</topic><topic>G6PD, glucose‐6‐phosphate dehydrogenase</topic><topic>gGT</topic><topic>gGT, g‐glutamyltranspeptidase</topic><topic>glucose-6-phosphate dehydrogenase</topic><topic>glutathione</topic><topic>Glutathione - metabolism</topic><topic>glutathione disulphide</topic><topic>glutathione peroxidase</topic><topic>glutathione reductase</topic><topic>glutathione S-transferase</topic><topic>GPx</topic><topic>GPx, glutathione peroxidase</topic><topic>GR, glutathione reductase</topic><topic>GSH</topic><topic>GSH, glutathione</topic><topic>GSSG</topic><topic>GSSG, glutathione disulphide</topic><topic>GST</topic><topic>GST, glutathione S‐transferase</topic><topic>SD, standard deviation</topic><topic>SOD</topic><topic>SOD, superoxide dismutase</topic><topic>standard deviation</topic><topic>superoxide dismutase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jürgensen, Claudia Würtz</creatorcontrib><creatorcontrib>Jacobsen, Nicklas Raun</creatorcontrib><creatorcontrib>Emri, Tamás</creatorcontrib><creatorcontrib>Havn Eriksen, Susanne</creatorcontrib><creatorcontrib>Pócsi, István</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of basic microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jürgensen, Claudia Würtz</au><au>Jacobsen, Nicklas Raun</au><au>Emri, Tamás</au><au>Havn Eriksen, Susanne</au><au>Pócsi, István</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glutathione metabolism and dimorphism in Aureobasidium pullulans</atitle><jtitle>Journal of basic microbiology</jtitle><addtitle>J. Basic Microbiol</addtitle><date>2001-05</date><risdate>2001</risdate><volume>41</volume><issue>2</issue><spage>131</spage><epage>137</epage><pages>131-137</pages><issn>0233-111X</issn><eissn>1521-4028</eissn><abstract>Yeast⟷mycelium morphological transitions of Aureobasidium pullulans are influenced by numerous environmental factors. In general, changes in the glutathione (GSH) metabolism of dimorphic fungi may lead to alterations in the reduced thiol status of the cells that are hypothesised to initialise morphological transitions. In accordance with this hypothesis, the specific GSH levels found in A. pullulans yeast cells were always significantly higher than those in mycelia. On the other hand, there was no significant difference between the GSH/GSSG redox status of the cells with either yeast or mycelial morphology. The cascade of events leading to morphological transitions was therefore unlikely to proceed via redox modulation of protein thiols. Although there were morphology‐dependent differences in the specific activities of some GSH metabolic enzymes, e.g. glutathione reductase (GR),γ‐glutamyltranspeptidase (γGT), glucose‐6‐phosphate dehydrogenase (G6PD), they were not satisfactory to explain the observed alterations in the intracellular GSH levels. It is noteworthy that very similar specific γGT and G6PD activities were found in cells separated from mixed morphology cultures independently of the actual cell morphology. On the other hand, the specific γGT and G6PD activities of A. pullulans cells sharing the same morphology but separated from pure and mixed morphology cultures showed marked differences.</abstract><cop>Berlin</cop><pub>WILEY-VCH Verlag Berlin GmbH</pub><pmid>11441460</pmid><doi>10.1002/1521-4028(200105)41:2<131::AID-JOBM131>3.0.CO;2-#</doi><tpages>7</tpages></addata></record> |
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subjects | Ascomycota - cytology Ascomycota - enzymology Ascomycota - growth & development Ascomycota - physiology Aureobasidium pullulans Culture Media g-glutamyltranspeptidase G6PD G6PD, glucose‐6‐phosphate dehydrogenase gGT gGT, g‐glutamyltranspeptidase glucose-6-phosphate dehydrogenase glutathione Glutathione - metabolism glutathione disulphide glutathione peroxidase glutathione reductase glutathione S-transferase GPx GPx, glutathione peroxidase GR, glutathione reductase GSH GSH, glutathione GSSG GSSG, glutathione disulphide GST GST, glutathione S‐transferase SD, standard deviation SOD SOD, superoxide dismutase standard deviation superoxide dismutase |
title | Glutathione metabolism and dimorphism in Aureobasidium pullulans |
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