PAS3, a Saccharomyces cerevisiae Gene Encoding a Peroxisomal Integral Membrane Protein Essential for Peroxisome Biogenesis
Saccharomyces cerevisiae pas3-mutants are described which conform the pas-phenotype recently reported for the peroxisomal assembly mutants pas1-1 and pas2. The isolation of pas3-mutants enabled us to clone the PAS3 gene by functional complementation. DNA sequence analysis revealed a 50.6-kD protein...
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| Veröffentlicht in: | The Journal of cell biology 1991-09, Vol.114 (6), p.1167-1178 |
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| container_title | The Journal of cell biology |
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| creator | Höhfeld, Jörg Veenhuis, Marten Wolf-H. Kunau |
| description | Saccharomyces cerevisiae pas3-mutants are described which conform the pas-phenotype recently reported for the peroxisomal assembly mutants pas1-1 and pas2. The isolation of pas3-mutants enabled us to clone the PAS3 gene by functional complementation. DNA sequence analysis revealed a 50.6-kD protein with at least one domain of sufficient length and hydrophobicity to span a lipid bilayer. To verify these predictions antibodies were raised against a truncated portion of the PAS3 coding region overexpressed in E. coli. Pas3p was identified as a 48 kD peroxisomal integral membrane protein. It is shown that a lack of this protein causes the peroxisome-deficient phenotype and the cytosolic mislocalization of peroxisomal matrix enzymes. Based on protease digestion experiments Pas3p is discussed to be anchored in the peroxisomal membrane by its amino-terminus while the bulk of the molecule is exposed to the cytosol. These findings are consistent with the possibility that Pas3p is one component of the peroxisomal import machinery. |
| doi_str_mv | 10.1083/jcb.114.6.1167 |
| format | Article |
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Kunau</creator><creatorcontrib>Höhfeld, Jörg ; Veenhuis, Marten ; Wolf-H. Kunau</creatorcontrib><description>Saccharomyces cerevisiae pas3-mutants are described which conform the pas-phenotype recently reported for the peroxisomal assembly mutants pas1-1 and pas2. The isolation of pas3-mutants enabled us to clone the PAS3 gene by functional complementation. DNA sequence analysis revealed a 50.6-kD protein with at least one domain of sufficient length and hydrophobicity to span a lipid bilayer. To verify these predictions antibodies were raised against a truncated portion of the PAS3 coding region overexpressed in E. coli. Pas3p was identified as a 48 kD peroxisomal integral membrane protein. It is shown that a lack of this protein causes the peroxisome-deficient phenotype and the cytosolic mislocalization of peroxisomal matrix enzymes. Based on protease digestion experiments Pas3p is discussed to be anchored in the peroxisomal membrane by its amino-terminus while the bulk of the molecule is exposed to the cytosol. These findings are consistent with the possibility that Pas3p is one component of the peroxisomal import machinery.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.114.6.1167</identifier><identifier>PMID: 1894692</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>New York, NY: Rockefeller University Press</publisher><subject>Amino Acid Sequence ; Antibodies ; ATP-Binding Cassette Transporters ; Base Sequence ; Biological and medical sciences ; Cells ; Cloning, Molecular ; Enzymes ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - genetics ; Fungal Proteins - isolation & purification ; Generally accepted auditing standards ; genes ; Genes, Fungal ; Genes. 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Kunau</creatorcontrib><title>PAS3, a Saccharomyces cerevisiae Gene Encoding a Peroxisomal Integral Membrane Protein Essential for Peroxisome Biogenesis</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Saccharomyces cerevisiae pas3-mutants are described which conform the pas-phenotype recently reported for the peroxisomal assembly mutants pas1-1 and pas2. The isolation of pas3-mutants enabled us to clone the PAS3 gene by functional complementation. DNA sequence analysis revealed a 50.6-kD protein with at least one domain of sufficient length and hydrophobicity to span a lipid bilayer. To verify these predictions antibodies were raised against a truncated portion of the PAS3 coding region overexpressed in E. coli. Pas3p was identified as a 48 kD peroxisomal integral membrane protein. It is shown that a lack of this protein causes the peroxisome-deficient phenotype and the cytosolic mislocalization of peroxisomal matrix enzymes. Based on protease digestion experiments Pas3p is discussed to be anchored in the peroxisomal membrane by its amino-terminus while the bulk of the molecule is exposed to the cytosol. These findings are consistent with the possibility that Pas3p is one component of the peroxisomal import machinery.</description><subject>Amino Acid Sequence</subject><subject>Antibodies</subject><subject>ATP-Binding Cassette Transporters</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cells</subject><subject>Cloning, Molecular</subject><subject>Enzymes</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - isolation & purification</subject><subject>Generally accepted auditing standards</subject><subject>genes</subject><subject>Genes, Fungal</subject><subject>Genes. Genome</subject><subject>Genetic Complementation Test</subject><subject>Genotype</subject><subject>Gin</subject><subject>Immunoblotting</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Microbodies - physiology</subject><subject>Microbodies - ultrastructure</subject><subject>Microscopy, Electron</subject><subject>Models, Structural</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>nucleotide sequence</subject><subject>P branes</subject><subject>Pas3p protein</subject><subject>Peroxins</subject><subject>Peroxisomes</subject><subject>Phenotype</subject><subject>Plasmids</subject><subject>Protein Conformation</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Restriction Mapping</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - physiology</subject><subject>Saccharomyces cerevisiae - ultrastructure</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Yeasts</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9rFDEcxYNY6rb16klhDtKTs83vSS5CLWtbqLhQPYdM5pttlplJm8wW619vyi5dPXlJAu_zfbxvHkLvCJ4TrNjZ2rVzQvhcllM2r9CMCI5rRTh-jWYYU1JrQcUbdJTzGmPMG84O0SFRmktNZ-j38vyWfapsdWudu7MpDk8OcuUgwWPIwUJ1CSNUi9HFLoyrAi4hxV8hx8H21fU4wSqVxzcY2mQLuExxgjBWi5xhnEKRfEz7Gai-hLgqjjnkE3TgbZ_h7e4-Rj-_Ln5cXNU33y-vL85vaicYnWrbSe8VI054bTFtPTBOG4W11QI7xbDTrbeeSNWJRnoAwhvNOkFlK7yQLTtGn7e-95t2gM6VXCWyuU9hsOnJRBvMv8oY7swqPhpKlSa0KQanO4MUHzaQJzOE7KDvy8Jxk01DCeZM_x8kEmupBCvgfAu6FHNO4F_SEGyeazWlVlNqNdI811oGPvy9wx7f9lj0jzvdZmd7X7pwIb9gXGvCOSnY-y22zlNMexdZ_kwS9gdZHLaK</recordid><startdate>19910901</startdate><enddate>19910901</enddate><creator>Höhfeld, Jörg</creator><creator>Veenhuis, Marten</creator><creator>Wolf-H. 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Kunau</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c532t-ad6ff831c5f9a02bfe3427809a950c830c9bfaf168d576fee14793d526b5f56b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Antibodies</topic><topic>ATP-Binding Cassette Transporters</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cells</topic><topic>Cloning, Molecular</topic><topic>Enzymes</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - isolation & purification</topic><topic>Generally accepted auditing standards</topic><topic>genes</topic><topic>Genes, Fungal</topic><topic>Genes. 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Kunau</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PAS3, a Saccharomyces cerevisiae Gene Encoding a Peroxisomal Integral Membrane Protein Essential for Peroxisome Biogenesis</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1991-09-01</date><risdate>1991</risdate><volume>114</volume><issue>6</issue><spage>1167</spage><epage>1178</epage><pages>1167-1178</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Saccharomyces cerevisiae pas3-mutants are described which conform the pas-phenotype recently reported for the peroxisomal assembly mutants pas1-1 and pas2. The isolation of pas3-mutants enabled us to clone the PAS3 gene by functional complementation. DNA sequence analysis revealed a 50.6-kD protein with at least one domain of sufficient length and hydrophobicity to span a lipid bilayer. To verify these predictions antibodies were raised against a truncated portion of the PAS3 coding region overexpressed in E. coli. Pas3p was identified as a 48 kD peroxisomal integral membrane protein. It is shown that a lack of this protein causes the peroxisome-deficient phenotype and the cytosolic mislocalization of peroxisomal matrix enzymes. Based on protease digestion experiments Pas3p is discussed to be anchored in the peroxisomal membrane by its amino-terminus while the bulk of the molecule is exposed to the cytosol. These findings are consistent with the possibility that Pas3p is one component of the peroxisomal import machinery.</abstract><cop>New York, NY</cop><pub>Rockefeller University Press</pub><pmid>1894692</pmid><doi>10.1083/jcb.114.6.1167</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of cell biology, 1991-09, Vol.114 (6), p.1167-1178 |
| issn | 0021-9525 1540-8140 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Antibodies ATP-Binding Cassette Transporters Base Sequence Biological and medical sciences Cells Cloning, Molecular Enzymes Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Fungal Proteins - genetics Fungal Proteins - isolation & purification Generally accepted auditing standards genes Genes, Fungal Genes. Genome Genetic Complementation Test Genotype Gin Immunoblotting Membrane proteins Membrane Proteins - genetics Membrane Proteins - isolation & purification Microbodies - physiology Microbodies - ultrastructure Microscopy, Electron Models, Structural Molecular and cellular biology Molecular genetics Molecular Sequence Data Molecular Weight nucleotide sequence P branes Pas3p protein Peroxins Peroxisomes Phenotype Plasmids Protein Conformation Recombinant Proteins - isolation & purification Restriction Mapping Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - physiology Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins Yeasts |
| title | PAS3, a Saccharomyces cerevisiae Gene Encoding a Peroxisomal Integral Membrane Protein Essential for Peroxisome Biogenesis |
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