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The role of ornithine aminotransferase in fruiting body formation of the mushroom Agaricus bisporus

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Wagemaker, Matthijs J. M., Eastwood, Daniel C., Welagen, Jelle, Van der Drift, Chris, Jetten, Mike S. M., Burton, Kerry S., Van Griensven, Leo J. L. D. and Den Campa, Huub J. M. Op (2007) The role of ornithine aminotransferase in fruiting body formation of the mushroom Agaricus bisporus. Mycological Research, Vol.111 (No.8). pp. 909-918. doi:10.1016/j.mycres.2007.05.012 ISSN 0953-7562.

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Official URL: http://dx.doi.org/10.1016/j.mycres.2007.05.012

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Abstract

The complete oat gene and cDNA from the commercial mushroom, Agaricus bisporus, encoding ornithine aminotransferase (OAT) was characterized. The gene encodes a 466 amino acid protein and provides the first fully reported homobasidiomycete OAT protein sequence. The gene is interrupted by ten introns, and no mitochondrial targeting motif was present pointing to a cytoplasmic localization. The function of the gene was demonstrated by complementation of a Saccharomyces cerevisiae mutant unable to utilize ornithine as a sole source of nitrogen with an A. bisporus oat cDNA construct. Northern analysis of the oat gene together with the pruA gene (encoding Δ1-pyrroline-5-carboxylate dehydrogenase) showed that transcripts of both genes were lower during the first stages of fruiting body development. The higher expression of the oat gene in later stages of development, suggests the importance of ornithine metabolism for the redistribution of metabolites in the developing mushroom. Hplc analysis of all amino acids revealed that ornithine levels increased during fruiting body development whereas proline levels fell.

Item Type: Journal Article
Subjects: Q Science > QK Botany
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) > Warwick HRI (2004-2010)
Journal or Publication Title: Mycological Research
Publisher: Cambridge University Press
ISSN: 0953-7562
Official Date: August 2007
Dates:
DateEvent
August 2007Published
Volume: Vol.111
Number: No.8
Number of Pages: 10
Page Range: pp. 909-918
DOI: 10.1016/j.mycres.2007.05.012
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

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