PDR5, a novel yeast multidrug resistance conferring transporter controlled by the transcription regulator PDR1

The complete sequence of the pleiotropic drug resistance gene PDR5 from Saccharomyces cerevisiae is reported and analyzed. PDR5 encodes a 160-kDa protein with a predicted duplicated six membrane-span domain and a repeated putative ATP-binding domain. PDR5 shares this structural feature with the mamm...

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Veröffentlicht in:The Journal of biological chemistry 1994-01, Vol.269 (3), p.2206-2214
Hauptverfasser: Balzi, E, Wang, M, Leterme, S, Dyck, L. van, Goffeau, A
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container_end_page 2214
container_issue 3
container_start_page 2206
container_title The Journal of biological chemistry
container_volume 269
creator Balzi, E
Wang, M
Leterme, S
Dyck, L. van
Goffeau, A
description The complete sequence of the pleiotropic drug resistance gene PDR5 from Saccharomyces cerevisiae is reported and analyzed. PDR5 encodes a 160-kDa protein with a predicted duplicated six membrane-span domain and a repeated putative ATP-binding domain. PDR5 shares this structural feature with the mammalian multidrug resistance pumps as well as the functional capacity of conferring resistance to various inhibitors upon amplification (Leppert, G., McDevitt, R., Falco, S.C., Van Dyk, T.K., Ficke, M.B., and Golin, J. (1990) Genetics 125, 13-20). The yeast PDR5 is thus a new member of the ABC (ATP-binding cassette) protein superfamily. Mutations in another yeast pleiotropic drug resistance gene, PDR1, encoding a putative transcription regulator (Balzi, E., Chen, W., Ulaszewski, S., Capieaux, E., and Goffeau, A. (1987) J. Biol. Chem. 262, 16871-16879), increase markedly the mRNA levels of the PDR5 and STE6 genes. The multidrug resistance mutations pdr1-3 and pdr1-6 also lead to considerable overexpression of the PDR5 plasma membrane protein
doi_str_mv 10.1016/s0021-9258(17)42155-7
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PDR5 encodes a 160-kDa protein with a predicted duplicated six membrane-span domain and a repeated putative ATP-binding domain. PDR5 shares this structural feature with the mammalian multidrug resistance pumps as well as the functional capacity of conferring resistance to various inhibitors upon amplification (Leppert, G., McDevitt, R., Falco, S.C., Van Dyk, T.K., Ficke, M.B., and Golin, J. (1990) Genetics 125, 13-20). The yeast PDR5 is thus a new member of the ABC (ATP-binding cassette) protein superfamily. Mutations in another yeast pleiotropic drug resistance gene, PDR1, encoding a putative transcription regulator (Balzi, E., Chen, W., Ulaszewski, S., Capieaux, E., and Goffeau, A. (1987) J. Biol. Chem. 262, 16871-16879), increase markedly the mRNA levels of the PDR5 and STE6 genes. 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PDR5 encodes a 160-kDa protein with a predicted duplicated six membrane-span domain and a repeated putative ATP-binding domain. PDR5 shares this structural feature with the mammalian multidrug resistance pumps as well as the functional capacity of conferring resistance to various inhibitors upon amplification (Leppert, G., McDevitt, R., Falco, S.C., Van Dyk, T.K., Ficke, M.B., and Golin, J. (1990) Genetics 125, 13-20). The yeast PDR5 is thus a new member of the ABC (ATP-binding cassette) protein superfamily. Mutations in another yeast pleiotropic drug resistance gene, PDR1, encoding a putative transcription regulator (Balzi, E., Chen, W., Ulaszewski, S., Capieaux, E., and Goffeau, A. (1987) J. Biol. Chem. 262, 16871-16879), increase markedly the mRNA levels of the PDR5 and STE6 genes. 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Psychology</topic><topic>Fungal Proteins - biosynthesis</topic><topic>Fungal Proteins - genetics</topic><topic>GENE</topic><topic>Gene Expression</topic><topic>GENES</topic><topic>Genes, Fungal</topic><topic>Glycoproteins</topic><topic>Humans</topic><topic>MEDICAMENT</topic><topic>MEDICAMENTOS</topic><topic>Membrane Proteins - biosynthesis</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - isolation &amp; purification</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>MUTACION</topic><topic>Mutagenesis</topic><topic>MUTATION</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>RESISTANCE AUX PRODUITS CHIMIQUES</topic><topic>RESISTENCIA QUIMICA</topic><topic>Restriction Mapping</topic><topic>RNA, Messenger - biosynthesis</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>SECUENCIA NUCLEICA</topic><topic>Sequence Homology, Amino Acid</topic><topic>SEQUENCE NUCLEIQUE</topic><topic>Terminator Regions, Genetic</topic><topic>Trans-Activators</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Balzi, E</creatorcontrib><creatorcontrib>Wang, M</creatorcontrib><creatorcontrib>Leterme, S</creatorcontrib><creatorcontrib>Dyck, L. van</creatorcontrib><creatorcontrib>Goffeau, A</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</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><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Balzi, E</au><au>Wang, M</au><au>Leterme, S</au><au>Dyck, L. van</au><au>Goffeau, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PDR5, a novel yeast multidrug resistance conferring transporter controlled by the transcription regulator PDR1</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-01-21</date><risdate>1994</risdate><volume>269</volume><issue>3</issue><spage>2206</spage><epage>2214</epage><pages>2206-2214</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The complete sequence of the pleiotropic drug resistance gene PDR5 from Saccharomyces cerevisiae is reported and analyzed. PDR5 encodes a 160-kDa protein with a predicted duplicated six membrane-span domain and a repeated putative ATP-binding domain. PDR5 shares this structural feature with the mammalian multidrug resistance pumps as well as the functional capacity of conferring resistance to various inhibitors upon amplification (Leppert, G., McDevitt, R., Falco, S.C., Van Dyk, T.K., Ficke, M.B., and Golin, J. (1990) Genetics 125, 13-20). The yeast PDR5 is thus a new member of the ABC (ATP-binding cassette) protein superfamily. Mutations in another yeast pleiotropic drug resistance gene, PDR1, encoding a putative transcription regulator (Balzi, E., Chen, W., Ulaszewski, S., Capieaux, E., and Goffeau, A. (1987) J. Biol. Chem. 262, 16871-16879), increase markedly the mRNA levels of the PDR5 and STE6 genes. The multidrug resistance mutations pdr1-3 and pdr1-6 also lead to considerable overexpression of the PDR5 plasma membrane protein</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8294477</pmid><doi>10.1016/s0021-9258(17)42155-7</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record>
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subjects ADENOSINE TRIPHOSPHATE
ADENOSINTRIFOSFATO
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
ATP-Binding Cassette Transporters
Base Sequence
Binding and carrier proteins
Biological and medical sciences
Carrier Proteins - biosynthesis
Carrier Proteins - chemistry
Carrier Proteins - genetics
Cloning, Molecular
DNA-Binding Proteins
Drug Resistance, Microbial - genetics
Fundamental and applied biological sciences. Psychology
Fungal Proteins - biosynthesis
Fungal Proteins - genetics
GENE
Gene Expression
GENES
Genes, Fungal
Glycoproteins
Humans
MEDICAMENT
MEDICAMENTOS
Membrane Proteins - biosynthesis
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - isolation & purification
Molecular Sequence Data
Molecular Weight
MUTACION
Mutagenesis
MUTATION
Protein Structure, Secondary
Proteins
RESISTANCE AUX PRODUITS CHIMIQUES
RESISTENCIA QUIMICA
Restriction Mapping
RNA, Messenger - biosynthesis
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins
SECUENCIA NUCLEICA
Sequence Homology, Amino Acid
SEQUENCE NUCLEIQUE
Terminator Regions, Genetic
Trans-Activators
Transcription Factors - metabolism
Transcription, Genetic
title PDR5, a novel yeast multidrug resistance conferring transporter controlled by the transcription regulator PDR1
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