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Isolation, characterization and molecular 3D model of human GDE4, a novel membrane protein containing glycerophosphodiester phosphodiesterase domain.
Molecular Membrane Biology Pub Date : 2008-11-11 , DOI: 10.1080/09687680802537605
Ping A Chang 1 , Hong B Shao , Ding X Long , Quan Sun , Yi J Wu
Affiliation  

As a transmembrane protein family, glycerophosphodiester phosphodiesterase (GDPD/GDE) catalyzes the hydrolysis of deacylated glycerophospholipids to glycerol phosphate and alcohol. To date, seven mammalian GDEs have been virtually cloned or predicted by bioinformatics analysis, however, GDE4 has not been molecular isolated and characterized in mammal. Here we report molecular cloning of human GDE4 encoding cDNA sequence, which is 945 base pairs long encoding a 314-amino acid protein with 2 transmembrane regions and a GDE motif. The human GDE1 gene is located on chromosome 19q22 and contains ten exons and nine introns. A molecular 3-D model provides the first structural information of human GDE4 and suggests a triose-phosphate-isomerase barrel core as typically found in bacterial GDPDs. Furthermore, a model of the putative catalytic residues highlights that the individual core residues Glu72, Asp74, and His87 are crucial to maintaining GDE4 catalytic activity. Western blotting shows that human GDE4 is a 36 kDa protein. Subcellular localization of GDE4 tagged with enhanced green fluorescence protein is in the cytoplasm, especially accumulated in the perinuclear region and the cell periphery. Moreover, over-expression of GDE4 did not induce neurite formation or change cell morphology. These results indicate GDE4 protein is a member of the GDE family and suggest it may play different roles from other members of GDE family.

中文翻译:

人GDE4的分离,表征和分子3D模型,一种新型膜蛋白,含有甘油磷酸二酯磷酸二酯酶结构域。

甘油磷酸二酯磷酸二酯酶(GDPD / GDE)作为跨膜蛋白家族,催化脱酰基甘油磷脂水解为磷酸甘油和乙醇。迄今为止,已经通过生物信息学分析虚拟地克隆或预测了七个哺乳动物GDE,但是,尚未在哺乳动物中分子分离和鉴定GDE4。在这里,我们报告了人类GDE4编码cDNA序列的分子克隆,该序列长945个碱基对,编码具有2个跨膜区域和GDE图案的314个氨基酸的蛋白质。人类GDE1基因位于19q22号染色体上,包含10个外显子和9个内含子。分子3-D模型提供了人类GDE4的第一个结构信息,并提出了在细菌GDPD中通常会发现的磷酸三糖-异构酶桶状核心。此外,推定的催化残基模型表明,单个核心残基Glu72,Asp74和His87对于维持GDE4催化活性至关重要。蛋白质印迹显示,人GDE4是一种36 kDa的蛋白质。用增强的绿色荧光蛋白标记的GDE4的亚细胞定位在细胞质中,尤其是在核周区域和细胞外围积累。此外,GDE4的过表达不会诱导神经突形成或改变细胞形态。这些结果表明GDE4蛋白是GDE家族的成员,并暗示它可能起与GDE家族其他成员不同的作用。用增强的绿色荧光蛋白标记的GDE4的亚细胞定位在细胞质中,尤其是在核周区域和细胞周围积累。此外,GDE4的过表达不会诱导神经突形成或改变细胞形态。这些结果表明GDE4蛋白是GDE家族的成员,并暗示它可能起与GDE家族其他成员不同的作用。用增强的绿色荧光蛋白标记的GDE4的亚细胞定位在细胞质中,尤其是在核周区域和细胞外围积累。此外,GDE4的过表达不会诱导神经突形成或改变细胞形态。这些结果表明GDE4蛋白是GDE家族的成员,并暗示它可能起与GDE家族其他成员不同的作用。
更新日期:2019-11-01
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