Isolation and characterization of acetoacetyl-CoA thiolase gene essential for n-decane assimilation in yeast Yarrowia lipolytica.
Biochem Biophys Res Commun
; 282(3): 832-8, 2001 Apr 06.
Article
em En
| MEDLINE
| ID: mdl-11401539
ABSTRACT
Yarrowia lipolytica is a yeast which can utilize n-alkane as a sole carbon source. We isolated a Y. lipolytica peroxisomal acetoacetyl-CoA thiolase gene, PAT1, by complementation of a mutant that cannot utilize n-decane as a sole carbon source. We found that the putative PAT1 product had conserved features of peroxisomal acetoacetyl-CoA thiolase. We showed that the PAT1 disruptant was not able to grow on n-decane, and that n-decane-inducible acetoacetyl-CoA thiolase activity largely depended on PAT1. The original mutant carried a mutation involving the replacement of Gly382 with Glu. This mutation inactivated the ability of PAT1 to complement the defective n-decane utilization of the disruptant. These results indicate that PAT1 encodes peroxisomal acetoacetyl-CoA thiolase and is essential for n-decane utilization in Y. lipolytica.
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Base de dados:
MEDLINE
Assunto principal:
Acetil-CoA C-Acetiltransferase
/
Alcanos
/
Saccharomycetales
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Genes Fúngicos
Idioma:
En
Ano de publicação:
2001
Tipo de documento:
Article