Oka Takuji, Hamaguchi Tetsu, Sameshima Yuka, Goto Masatoshi, Furukawa Kensuke
Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka 812-8581, Japan.
Microbiology (Reading). 2004 Jun;150(Pt 6):1973-1982. doi: 10.1099/mic.0.27005-0.
Protein O-glycosylation is essential for protein modification and plays important roles in eukaryotic cells. O-Mannosylation of proteins occurs in the filamentous fungus Aspergillus. The structure and function of the pmtA gene, encoding protein O-d-mannosyltransferase, which is responsible for the initial O-mannosylation reaction in Aspergillus nidulans, was characterized. Disruption of the pmtA gene resulted in the reduction of in vitro protein O-d-mannosyltransferase activity to 6 % of that of the wild-type strain and led to underglycosylation of an extracellular glucoamylase. The pmtA disruptant exhibited abnormal cell morphology and alteration in carbohydrate composition, particularly reduction in the skeletal polysaccharides in the cell wall. The results indicate that PmtA is required for the formation of a normal cell wall in A. nidulans.
蛋白质O-糖基化对于蛋白质修饰至关重要,在真核细胞中发挥着重要作用。蛋白质的O-甘露糖基化发生在丝状真菌曲霉中。对编码蛋白质O-D-甘露糖基转移酶的pmtA基因的结构和功能进行了表征,该酶负责构巢曲霉中的初始O-甘露糖基化反应。pmtA基因的破坏导致体外蛋白质O-D-甘露糖基转移酶活性降低至野生型菌株的6%,并导致细胞外糖化酶的糖基化不足。pmtA disruptant表现出异常的细胞形态和碳水化合物组成的改变,特别是细胞壁中骨架多糖的减少。结果表明,PmtA是构巢曲霉正常细胞壁形成所必需的。