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

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 i...

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Bibliographic Details
Published in:FEMS yeast research 2002, Vol.1 (4), p.257-263
Main Authors: van Dijk, Ralf, Lahchev, Kancho L, Kram, Anita M, van der Klei, Ida J, Veenhuis, Marten
Format: Article
Language:English
Subjects:
Alcohol oxidase
Hansenula polymorpha
Peroxisome
Protein assembly
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Summary: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.
ISSN:1567-1356
1567-1364
DOI:10.1016/S1567-1356(01)00038-1