The transporters Pdr5p and Snq2p mediate diazaborine resistance and are under the control of the gain‐of‐function allele PDR1‐12
The spontaneous acquisition of resistance to a variety of unrelated cytotoxic compounds has important implications in medical treatment of infectious diseases and anticancer therapy. In the yeast Saccharomyces cerevisiae this phenomenon is caused by overexpression of membrane efflux pumps and is cal...
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| Veröffentlicht in: | European journal of biochemistry 2004-03, Vol.271 (6), p.1145-1152 |
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| creator | Wehrschütz‐Sigl, Eva Jungwirth, Helmut Bergler, Helmut Högenauer, Gregor |
| description | The spontaneous acquisition of resistance to a variety of unrelated cytotoxic compounds has important implications in medical treatment of infectious diseases and anticancer therapy. In the yeast Saccharomyces cerevisiae this phenomenon is caused by overexpression of membrane efflux pumps and is called pleiotropic drug resistance. We have found that allelic forms of the genes for the transcription activators Pdr1p and Pdr3p, designated PDR1‐12 and PDR3‐33, respectively, mediate resistance to diazaborine. Here we demonstrate that the transporters Pdr5p and Snq2p are involved in diazaborine detoxification. We report that in the PDR3‐33 mutant diazaborine resistance is exerted mainly via overexpression of the PDR5 and SNQ2 genes, while in the PDR1‐12 mutant, additional genes, i.e. the Yap1p target genes FLR1 and YCF1, are also involved in diazaborine detoxification. In addition, we show that in the presence of cycloheximide or diazaborine PDR5 can be activated by additional transcription factors beside Pdr1p and Pdr3p. |
| doi_str_mv | 10.1111/j.1432-1033.2004.04018.x |
| format | Article |
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In the yeast Saccharomyces cerevisiae this phenomenon is caused by overexpression of membrane efflux pumps and is called pleiotropic drug resistance. We have found that allelic forms of the genes for the transcription activators Pdr1p and Pdr3p, designated PDR1‐12 and PDR3‐33, respectively, mediate resistance to diazaborine. Here we demonstrate that the transporters Pdr5p and Snq2p are involved in diazaborine detoxification. We report that in the PDR3‐33 mutant diazaborine resistance is exerted mainly via overexpression of the PDR5 and SNQ2 genes, while in the PDR1‐12 mutant, additional genes, i.e. the Yap1p target genes FLR1 and YCF1, are also involved in diazaborine detoxification. 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In the yeast Saccharomyces cerevisiae this phenomenon is caused by overexpression of membrane efflux pumps and is called pleiotropic drug resistance. We have found that allelic forms of the genes for the transcription activators Pdr1p and Pdr3p, designated PDR1‐12 and PDR3‐33, respectively, mediate resistance to diazaborine. Here we demonstrate that the transporters Pdr5p and Snq2p are involved in diazaborine detoxification. We report that in the PDR3‐33 mutant diazaborine resistance is exerted mainly via overexpression of the PDR5 and SNQ2 genes, while in the PDR1‐12 mutant, additional genes, i.e. the Yap1p target genes FLR1 and YCF1, are also involved in diazaborine detoxification. In addition, we show that in the presence of cycloheximide or diazaborine PDR5 can be activated by additional transcription factors beside Pdr1p and Pdr3p.</description><subject>ABC transporters</subject><subject>Adaptor Proteins, Signal Transducing</subject><subject>Alleles</subject><subject>ATP-Binding Cassette Transporters - genetics</subject><subject>ATP-Binding Cassette Transporters - metabolism</subject><subject>Aza Compounds - metabolism</subject><subject>Aza Compounds - pharmacology</subject><subject>Blotting, Northern</subject><subject>Boron Compounds - metabolism</subject><subject>Boron Compounds - pharmacology</subject><subject>Carrier Proteins - metabolism</subject><subject>Cycloheximide - pharmacology</subject><subject>diazaborine</subject><subject>Drug Resistance</subject><subject>Membrane Transport Proteins</subject><subject>Organic Anion Transporters</subject><subject>RNA, Messenger - biosynthesis</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - drug effects</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><subject>Transcriptional Activation</subject><subject>transcriptional regulation</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkctu1DAUhi0EokPhFZBX7JKe4zgXb5CgN5AqUdGytjzOCWSUsVM7ES0rVqx5Rp4EZ2YES_DCPra_81vyxxhHyDGNk02OshAZQlHkAkDmIAGb_P4RW_25eMxWACgzocrqiD2LcQMAlarqp-wISwCFqlixH7dfiE_BuDj6MFGI_LoN5ciNa_mNuxMj31Lbm4l4mr-ZtQ-9Ix4o9nEyztIONIH47FoKfEpp1rsp-IH7brf9bHr36_tP36Wpm52deu-4GQYaiF-ffcR0jOI5e9KZIdKLw3rMPl2c356-y64-XL4_fXOV2RKLJlOyhrrEhiQV0BrZ1CCMgKpthLRCWNEY0VhCMuuSlKgqKIVR1RpTpUStimP2ap87Bn83U5z0to-WhsE48nPUNdZFraT8J4iJwn1iswdt8DEG6vQY-q0JDxpBL7L0Ri9O9OJEL7L0Tpa-T60vD2_M6_TLfxsPdhLweg987Qd6-O9gfXH-9mYpi98AHKTA</recordid><startdate>200403</startdate><enddate>200403</enddate><creator>Wehrschütz‐Sigl, Eva</creator><creator>Jungwirth, Helmut</creator><creator>Bergler, Helmut</creator><creator>Högenauer, Gregor</creator><general>Blackwell Science Ltd</general><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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200403</creationdate><title>The transporters Pdr5p and Snq2p mediate diazaborine resistance and are under the control of the gain‐of‐function allele PDR1‐12</title><author>Wehrschütz‐Sigl, Eva ; Jungwirth, Helmut ; Bergler, Helmut ; Högenauer, Gregor</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5138-94707518e4e30da48702a206d824c22c28a28ce1eab5e9266052a96b166092793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>ABC transporters</topic><topic>Adaptor Proteins, Signal Transducing</topic><topic>Alleles</topic><topic>ATP-Binding Cassette Transporters - genetics</topic><topic>ATP-Binding Cassette Transporters - metabolism</topic><topic>Aza Compounds - metabolism</topic><topic>Aza Compounds - pharmacology</topic><topic>Blotting, Northern</topic><topic>Boron Compounds - metabolism</topic><topic>Boron Compounds - pharmacology</topic><topic>Carrier Proteins - metabolism</topic><topic>Cycloheximide - pharmacology</topic><topic>diazaborine</topic><topic>Drug Resistance</topic><topic>Membrane Transport Proteins</topic><topic>Organic Anion Transporters</topic><topic>RNA, Messenger - biosynthesis</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - drug effects</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Transcriptional Activation</topic><topic>transcriptional regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wehrschütz‐Sigl, Eva</creatorcontrib><creatorcontrib>Jungwirth, Helmut</creatorcontrib><creatorcontrib>Bergler, Helmut</creatorcontrib><creatorcontrib>Högenauer, Gregor</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wehrschütz‐Sigl, Eva</au><au>Jungwirth, Helmut</au><au>Bergler, Helmut</au><au>Högenauer, Gregor</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The transporters Pdr5p and Snq2p mediate diazaborine resistance and are under the control of the gain‐of‐function allele PDR1‐12</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>2004-03</date><risdate>2004</risdate><volume>271</volume><issue>6</issue><spage>1145</spage><epage>1152</epage><pages>1145-1152</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>The spontaneous acquisition of resistance to a variety of unrelated cytotoxic compounds has important implications in medical treatment of infectious diseases and anticancer therapy. In the yeast Saccharomyces cerevisiae this phenomenon is caused by overexpression of membrane efflux pumps and is called pleiotropic drug resistance. We have found that allelic forms of the genes for the transcription activators Pdr1p and Pdr3p, designated PDR1‐12 and PDR3‐33, respectively, mediate resistance to diazaborine. Here we demonstrate that the transporters Pdr5p and Snq2p are involved in diazaborine detoxification. We report that in the PDR3‐33 mutant diazaborine resistance is exerted mainly via overexpression of the PDR5 and SNQ2 genes, while in the PDR1‐12 mutant, additional genes, i.e. the Yap1p target genes FLR1 and YCF1, are also involved in diazaborine detoxification. 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| subjects | ABC transporters Adaptor Proteins, Signal Transducing Alleles ATP-Binding Cassette Transporters - genetics ATP-Binding Cassette Transporters - metabolism Aza Compounds - metabolism Aza Compounds - pharmacology Blotting, Northern Boron Compounds - metabolism Boron Compounds - pharmacology Carrier Proteins - metabolism Cycloheximide - pharmacology diazaborine Drug Resistance Membrane Transport Proteins Organic Anion Transporters RNA, Messenger - biosynthesis Saccharomyces cerevisiae Saccharomyces cerevisiae - drug effects Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Transcription Factors - genetics Transcription Factors - metabolism Transcriptional Activation transcriptional regulation |
| title | The transporters Pdr5p and Snq2p mediate diazaborine resistance and are under the control of the gain‐of‐function allele PDR1‐12 |
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