Two novel annexins from Drosophila melanogaster. Cloning, characterization, and differential expression in development.
Two novel annexins from Drosophila melanogaster. Cloning, characterization, and differential expression in development.
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DOI：
10.1016/s0021-9258(19)38604-1
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发表时间：
1990-07
期刊：
影响因子：
--
通讯作者：
P. Johnston;M. Perin;G. A. Reynolds;S. Wasserman;T. Südhof
中科院分区：
文献类型：
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作者：
P. Johnston;M. Perin;G. A. Reynolds;S. Wasserman;T. Südhof
膜联蛋白是同源 Ca2(+)- 和磷脂结合蛋白家族，迄今为止仅在脊椎动物中发现。分离并表征了编码来自黑腹果蝇的两种新型膜联蛋白的 cDNA 克隆。 RNA印迹表明，两种果蝇蛋白的信息在发育过程中表达存在差异，其中一种信息在整个发育过程中表达，而另一种信息仅在早期胚胎和成年果蝇中发现。原位杂交将两个果蝇基因定位于93B和19A-4,7。果蝇膜联蛋白与不同脊椎动物膜联蛋白具有类似的高度同源性，表明果蝇膜联蛋白不是特定哺乳动物膜联蛋白的无脊椎动物同源物，而是它们构成膜联蛋白基因家族的新成员。延续最近建立的术语，果蝇膜联蛋白将被命名为膜联蛋白 IX 和 X。使用重组蛋白研究果蝇膜联蛋白 X 的生化特性。与脊椎动物膜联蛋白类似，膜联蛋白 X 以钙依赖性方式与肝膜和含有磷脂酰丝氨酸的脂质体结合，但不与含有磷脂酰胆碱的脂质体结合。此外，膜联蛋白 X 根据钙的作用分配到 Triton X-114 的去污剂相中。无脊椎动物中Ca2+结合蛋白膜联蛋白家族的保守性表明它们在细胞中具有脊椎动物生物学所不特有的基本功能，并且果蝇序列的可用性将为这些功能的突变研究开辟途径。
The annexins are a family of homologous Ca2(+)- and phospholipid-binding proteins that until now have only been found in vertebrates. cDNA clones encoding two novel annexins from Drosophila melanogaster were isolated and characterized. RNA blots indicate that the messages for the two Drosophila proteins are differentially expressed in development, with one message being expressed throughout development, while the other is only found in early embryos and adult flies. In situ hybridizations localize the two Drosophila genes to 93B and 19A-4,7. A similarly high degree of homology relates Drosophila annexins to different vertebrate annexins, indicating that the Drosophila annexins are not the invertebrate homologues of particular mammalian annexins but that they constitute novel members of the annexin gene family. In continuation with a recently established terminology, the Drosophila annexins will be named annexins IX and X. The biochemical properties of Drosophila annexin X were investigated using recombinant protein. Similar to vertebrate annexins, annexin X bound to liver membranes and liposomes containing phosphatidylserine in a calcium-dependent manner but not to liposomes containing phosphatidylcholine. In addition, annexin X partitioned into the detergent phase of Triton X-114 as a function of calcium. The conservation of the annexin family of Ca2(+)-binding proteins in invertebrates suggests that they have a basic function in cells which is not peculiar to vertebrate biology, and the availability of the Drosophila sequences will open avenues for mutational studies of these functions.