title: The birth of yeast peroxisomes.
abstract: This contribution describes the phenotypic differences of yeast peroxisome-deficient mutants (pex mutants). In some cases different phenotypes were reported for yeast mutants deleted in the same PEX gene. These differences are most likely related to the marker proteins and methods used to detect peroxisomal remnants. This is especially evident for pex3 and pex19 mutants, where the localization of receptor docking proteins (Pex13, Pex14) resulted in the identification of peroxisomal membrane remnants, which do not contain other peroxisomal membrane proteins, such as the ring proteins Pex2, Pex10 and Pex12. These structures in pex3 and pex19 cells are the template for peroxisome formation upon introduction of the missing gene. Taken together, these data suggest that in all yeast pex mutants analyzed so far peroxisomes are not formed de novo but use membrane remnant structures as a template for peroxisome formation upon reintroduction of the missing gene. The relevance of this model for peroxisomal membrane protein and lipid sorting to peroxisomes is discussed.
authors.affiliation: Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, the Netherlands.
authors.forename: Wei
authors.initials: W
authors.lastname: Yuan
authors.affiliation: Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, the Netherlands.
authors.forename: Marten
authors.initials: M
authors.lastname: Veenhuis
authors.affiliation: Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, the Netherlands. Electronic address: I.J.van.der.klei@rug.nl.
authors.forename: Ida J
authors.initials: IJ
authors.lastname: van der Klei
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000737:chemistry / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000737:chemistry / Q000378:metabolism; D005786:Gene Expression Regulation; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001678:Organelle Biogenesis; D000074401:Peroxins; D020675:Peroxisomes / Q000737:chemistry / Q000378:metabolism*; D010944:Plants / Q000737:chemistry / Q000378:metabolism; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D015003:Yeasts / Q000737:chemistry / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; C109779:PEX19 protein, S cerevisiae; C070895:PEX3 protein, S cerevisiae; D000074401:Peroxins; D020033:Protein Isoforms; D029701:Saccharomyces cerevisiae Proteins
keywords: Lipids; Membrane; Membrane contact sites; Peroxisomal membrane protein; Peroxisome; Peroxisome-deficient mutant; Yeast