Enlarged peroxisomes are present in oleic acid-grown Yarrowia lipolytica overexpressing the PEX16 gene encoding an intraperoxisomal peripheral membrane peroxin

• Published in: The Journal of cell biology 1997-06, Vol.137 (6), p.1265-1278
• Main Authors: Eitzen, G.A. (University of Alberta, Edmonton, Canada.), Szilard, R.K, Rachubinski, R.A
• Format: Article
• Language: English
• Subjects: ACIDE OLEIQUE; ACIDO OLEICO; Amino Acid Sequence; Amino acids; Animals; Antibodies; Base Sequence; Carboxylic Acids; Cells; Cellular biology; COMPOSICION QUIMICA; COMPOSITION CHIMIQUE; DIMENSION; DISPONIBILIDAD DE NUTRIENTES; DISPONIBILITE D'ELEMENT NUTRITIF; DNA, Fungal; ENDOMYCETALES; ESTRUCTURA CELULAR; EXPRESION GENICA; EXPRESSION DES GENES; Extracellular Matrix - metabolism; Fungal Proteins - genetics; Fungal Proteins - metabolism; GENE; Gene Expression; Generally accepted auditing standards; GENES; Genes, Fungal; Guinea Pigs; IMMUNOLOGIE; INMUNOLOGIA; MEMBRANAS CELULARES; MEMBRANE CELLULAIRE; Membrane proteins; Membrane Proteins - genetics; Membrane Proteins - metabolism; Membranes; METABOLISME DES PROTEINES; METABOLISMO PROTEICO; Microbodies; Molecular Sequence Data; MUTANT; MUTANTES; Oleic Acid - pharmacology; Open reading frames; ORGANITE CELLULAIRE; ORGANULOS CITOPLASMICOS; Peroxisomes; Plasmids; PROTEINAS; PROTEINE; Rabbits; Saccharomycetales - genetics; Saccharomycetales - growth & development; Saccharomycetales - metabolism; Saccharomycetales - ultrastructure; SECUENCIA NUCLEOTIDICA; SEQUENCE NUCLEOTIDIQUE; SINTESIS DE PROTEINAS; STRUCTURE CELLULAIRE; SYNTHESE PROTEIQUE; ULTRAESTRUCTURA; ULTRASTRUCTURE; Yarrowia; Yeast; Yeasts; Yeasts - genetics; Yeasts - growth & development; Yeasts - metabolism; Yeasts - ultrastructure
• ISSN: 0021-9525; 1540-8140
• DOI: 10.1083/jcb.137.6.1265

Pex mutants of the yeast Yarrowia lipolytica are defective in peroxisome assembly. The mutant strain pex16-1 lacks morphologically recognizable peroxisomes. Most peroxisomal proteins are mislocalized to a subcellular fraction enriched for cytosol in pex16 strains, but a subset of peroxisomal proteins is localized at, or near, wild-type levels to a fraction typically enriched for peroxisomes. The PEX16 gene was isolated by functional complementation of the pex16-1 strain and encodes a protein, Pex16p, of 391 amino acids (44,479 D). Pex16p has no known homologues. Pex16p is a peripheral protein located at the matrix face of the peroxisomal membrane. Substitution of the carboxyl-terminal tripeptide Ser-Thr-Leu, which is similar to the consensus sequence of peroxisomal targeting signal 1, does not affect targeting of Pex16p to peroxisomes. Pex16p is synthesized in wild-type cells grown in glucose-containing media, and its levels are modestly increased by growth of cells in oleic acid-containing medium. Overexpression of the PEX16 gene in oleic acid-grown Y. lipolytica leads to the appearance of a small number of enlarged peroxisomes, which contain the normal complement of peroxisomal proteins at levels approaching those of wild-type peroxisomes