Biochemical characterization of a byssal protein from Dreissena bugensis (Andrusov)
Biochemical characterization of a byssal protein from Dreissena bugensis (Andrusov)
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DOI：
10.1080/08927010290017716
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发表时间：
2002-03-01
期刊：
影响因子：
2.7
通讯作者：
Waite, JH
中科院分区：
文献类型：
--
作者：
Anderson, KE;Waite, JH
Dreissena bugensis 足蛋白 1 (Dbfp1) 是一种串联重复、含多巴的蛋白质，从斑驴 Dreissena bugensis (Andrusov) 的足部分离出来，Dbfp1 是一种酸性糖蛋白，含有与苏氨酸残基 O 连接的单糖 N-乙酰半乳糖胺 (N-GaINAc)。一级序列数据表明，该蛋白质部分由富含甘氨酸的独特重复八肽基序组成。 Dbfp1 与 Dpfp1（来自同属斑马贻贝 Dreissena polymorpha (Pallas) 的足丝前体）相似，因为这两种蛋白质都含有肽基多巴，具有酸性等电点，并被 N-GaINAc 糖基化。然而，Dbfp1 的八肽基序与地精中发现的重复序列基序不同。 Dbfp1 中肽多巴的检测进一步强化了这样的假设：淡水德莱森鱼采用了与海洋贻贝所采用的基本相似的粘附策略。
The biochemical characterization of Dreissena bugensis foot protein 1 (Dbfp1), a tandemly repetitive, Dopa-containing protein isolated from the foot of the quagga mussel, Dreissena bugensis (Andrusov) is described, Dbfp1 is an acidic glycoprotein containing N-acetylgalactosamine (N-GaINAc) O-linked to threonine residues as a monosaccharide. Primary sequence data reveal that the protein is partly composed of a unique, repeating octapeptide motif rich in glycine. Dbfp1 resembles Dpfp1, a byssal precursor from the congeneric zebra mussel, Dreissena polymorpha (Pallas), in that both proteins contain peptidyl-Dopa, have acidic isoelectric points, and are glycosylated with N-GaINAc. However, the octapeptide motif of Dbfp1 differs from repetitive sequence motifs found in D. polymorpha. The detection of peptidy-Dopa in Dbfp1 further strengthens the hypothesis that the freshwater dreissenids have adopted an adhesive strategy fundamentally similar to that employed by marine mussels.