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MBC in Press, published online ahead of print November 18, 2002
Mol. Biol. Cell 10.1091/mbc.E02-07-0417

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Submitted on July 22, 2002
Revised on October 16, 2002
Accepted on October 28, 2002

Pyruvate carboxylase is an essential protein in the assembly of yeast peroxisomal oligomeric alcohol oxidase

Paulina Ozimek1, Ralf van Dijk1, Kantcho Latchev2, Carlos Gancedo3, Dong Yuan Wang1, Ida J. van der Klei1, and Marten Veenhuis1*

1 Eukaryotic Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, P.O. Box 14, 9750 AA Haren, The Netherlands
2 Institute of Microbiology, Bulgarian Academy of Sciences, Sofia, Bulgaria
3 Instituto de Investigaciones Biomédicas C.S.I.C., Madrid, Spain

* Corresponding author. E-mail address: M.Veenhuis{at}biol.rug.nl.

Hansenula polymorpha ass3 mutants are characterized by the accumulation of inactive alcohol oxidase (AO) monomers in the cytosol, while other peroxisomal matrix proteins are normally activated and sorted to peroxisomes. These mutants also have a glutamate or aspartate requirement on minimal media. Cloning of the corresponding gene resulted in the isolation of the H. polymorpha PYC gene that encodes pyruvate carboxylase (HpPyc1p).

HpPyc1p is a cytosolic, anapleurotic enzyme that replenishes the tricarboxylic acid cycle with oxaloacetate. The absence of this enzyme can be compensated by addition of aspartate or glutamate to the growth media.

We show that HpPyc1p protein, but not the enzyme activity is essential for import and assembly of AO. Similar results were obtained in the related yeast Pichia pastoris. In vitro studies revealed that HpPyc1p has affinity for FAD and is capable to physically interact with AO protein. These data suggest that in methylotrophic yeast pyruvate carboxylase plays a dual role in that, besides its well-characterized metabolic function as anapleurotic enzyme, the protein fulfils a specific role in the AO sorting and assembly process, possibly by mediating FAD-binding to AO monomers.




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