Isolation of mutants of Hansenula polymorpha defective in the assembly of octameric alcohol oxidase

Ralf van Dijk, Kancho L. Lahchev, Anita M. Kram, Ida J. van der Klei, Marten Veenhuis

OnderzoeksoutputAcademic

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Samenvatting

Alcohol oxidase (AO) is a peroxisomal enzyme that catalyses the first step in methanol metabolism in yeast. Monomeric, inactive AO protein is synthesised in the cytosol and subsequently imported into peroxisomes, where the enzymatically active, homo-octameric form is found. The mechanisms involved in AO octamer assembly are largely unclear. Here we describe the isolation of Hansenula polymorpha mutants specifically affected in AO assembly. These mutants are unable to grow on methanol and display reduced AO activities. Based on their phenotypes, three major classes of mutants were isolated. Three additional mutants were isolated that each displayed a unique phenotype. Complementation analysis revealed that the isolated AO assembly mutants belonged to 10 complementation groups.
Originele taal-2English
Aantal pagina's7
TijdschriftFems Yeast Research
Volume1
Nummer van het tijdschrift4
DOI's
StatusPublished - 2002

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