Enlarged peroxisomes are present in oleic acid-grown Yarrowia lipolytica overexpressing the PEX16 gene encoding an intraperoxisomal peripheral membrane peroxin.
J Cell Biol
; 137(6): 1265-78, 1997 Jun 16.
Article
em En
| MEDLINE
| ID: mdl-9182661
ABSTRACT
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 carboxylterminal 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.
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Base de dados:
MEDLINE
Assunto principal:
Leveduras
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Proteínas Fúngicas
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Saccharomycetales
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Proteínas de Membrana
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Microcorpos
Limite:
Animals
Idioma:
En
Revista:
J Cell Biol
Ano de publicação:
1997
Tipo de documento:
Article
País de afiliação:
Canadá