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Protein O-mannosyltransferase A of Aspergillus awamori is involved in O-mannosylation of glucoamylase I

Takuji Oka

Yuka Sameshima

Hoon Kim

Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Hakozaki 6-10-1, Fukuoka 812-8581, Japan

Correspondence
Kensuke Furukawa
kfurukaw{at}agr.kyushu-u.ac.jp

Industrially important extracellular enzymes from filamentous fungi are often O-mannosylated. The structure and function of the pmtA (AapmtA) gene encoding the protein O-D-mannosyltransferase of Aspergillus awamori were characterized. The AapmtA disruptant, designated AaPMTA, was constructed by homologous recombination. The strain AaPMTA exhibited fragile cell morphology with respect to hyphal extension, as well as swollen hyphae formation and conidia formation in potato dextrose medium. Moreover, the AapmtA disruptant showed increased sensitivity to high temperature and Congo red. Thus, the AaPmtA protein is involved in the formation of the normal cell wall. The strain AaPMTA could grow well in liquid synthetic medium and secrete glucoamylase I (GAI-AaPMTA) to a similar extent to the wild-type strain (GAI-WT). Matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis of the GAIs revealed that approximately 33 mannose moieties of GAI were absent in strain AaPMTA. This result indicates that the AaPmtA protein is responsible for the transfer of mannose to GAI. Structural analysis of the O-linked oligosaccharides of GAI also demonstrated that the AapmtA disruption resulted in a reduction of the amounts of O-linked oligosaccharides, such as D-mannose and -1,2-mannotriose, in GAI-AaPMTA. However, the amount of -1,2-mannobiose was comparable between GAI-WT and GAI-AaPMTA. The result suggests the presence of a compensatory mechanism in the synthetic pathway of O-mannosylation in A. awamori.

The GenBank/EMBL/DDBJ accession number for the AapmtA sequence reported in this paper is AF396953.

Present address: Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan.

Present address: Department of Biotechnology, Osaka University, Osaka, Japan.

Present address: Department of Agricultural Chemistry, Sunchon National University, Korea.

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