Kim H R, Yew N S, Ansorge W, Voss H, Schwager C, Vennström B, Zenke M, Engel J D
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208.
Mol Cell Biol. 1988 Oct;8(10):4416-24. doi: 10.1128/mcb.8.10.4416-4424.1988.
The chicken erythrocyte anion transport protein (band 3 of the erythrocyte cytoskeleton) is a central component taking part in two widely divergent functions of erythroid cells; it is a primary determinant of cytoskeletal architecture and responsible for electroneutral Cl-/HCO3- exchange across the plasma membrane. To analyze interesting aspects of the developmental regulation of this gene, we have cloned the cDNA and genomic counterparts of the erythroid-specific anion transport protein. We show that a single genetic locus for band 3 encodes two different erythroid cell-specific mRNAs, with different translational initiation sites, which predict polypeptides of sizes very close to those observed in vivo. In vitro translation and immune precipitation of synthetic mRNA derived from one putative fully encoding cDNA clone demonstrate that this clone gives rise to a protein which is identical in size and antigenicity to bona fide chicken erythroid band 3.
鸡红细胞阴离子转运蛋白(红细胞细胞骨架的带3蛋白)是参与红细胞两种截然不同功能的核心成分;它是细胞骨架结构的主要决定因素,并负责跨质膜的电中性Cl⁻/HCO₃⁻交换。为了分析该基因发育调控的有趣方面,我们克隆了红细胞特异性阴离子转运蛋白的cDNA和基因组对应物。我们发现,带3蛋白的单个基因位点编码两种不同的红细胞特异性mRNA,它们具有不同的翻译起始位点,预测的多肽大小与体内观察到的非常接近。对来自一个假定的完全编码cDNA克隆的合成mRNA进行体外翻译和免疫沉淀表明,该克隆产生的蛋白质在大小和抗原性上与真正的鸡红细胞带3蛋白相同。