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Glycobiology Advance Access published online on July 24, 2003
Glycobiology, doi:10.1093/glycob/cwg099
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Submitted on October 25, 2002
Revised on June 30, 2003
Accepted on June 30, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

Interaction of GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase with GDP-mannose-4,6-dehydratase stabilizes the enzyme activity for formation of GDP-fucose from GDP-mannose

Ken-ichi Nakayama 1, Yumi Maeda 1, and Yoshifumi Jigami 1*

1 Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba Central 6, 1-1 Higashi, Tsukuba 305-8566, Japan

* To whom correspondence should be addressed. E-mail: jigami.yoshi{at}aist.go.jp.

Abstract

We cloned GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase gene from Arabidopsis thaliana (AtFX/GER1). The yeast Saccharomyces cerevisiae was transfected with AtFX/GER1 gene, co-expressed with GDP-mannose-4,6-dehydratase gene of A. thaliana (MUR1). In vitro GDP-fucose synthesis activity was observed in the cytoplasmic fraction of cells co-expressing AtFX/GER1 gene and MUR1 gene. However, the cytoplasmic fraction of cells expressing MUR1 alone did not show the GDP-mannose-4,6-dehydratase activity. This result suggests that AtFX/GER1 protein may contribute to maintenance of MUR1 protein as the active form. Immunoprecipitation experiments showed that both proteins interact with each other, indicating that this interaction is required to maintain MUR1 protein as the active or stable form. Finally, in vivo GDP-fucose synthesis activity was analyzed by measuring the amount of GDP-fucose produced in cytoplasm of yeast cells. The amount of GDP-fucose in cells co-expressing MUR1 and AtFX/GER1 genes was 3.5 times higher than the amount of GDP-mannose in the same cells, indicating that this co-expression system is suitable for production of the valuable sugar nucleotide GDP-fucose in yeast.


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