Negrini C, Rivolta M N, Kalinec F, Kachar B
Laboratory of Cellular Biology, National Institute on Deafness and other Communication Disorders, National Institutes of Health, Rockville, MD 20850, USA.
Biochim Biophys Acta. 1995 May 24;1236(1):207-11. doi: 10.1016/0005-2736(95)00081-d.
We have isolated a cDNA clone from a guinea pig organ of Corti library encoding a new isoform of the Anion Exchanger 2 (AE2) protein. This cDNA clone shows an 83 bp deletion in the region that encodes the membrane domain of AE2. Analysis of the overlapping regions of genomic and cDNA clones indicates that the missing portion does not correspond exactly to a constitutive exon. The alternate splicing process that generates this transcript involves internal donor and acceptor sites which introduces a shift in the open reading frame. The resulting polypeptide has a conserved cytoplasmic N-terminal domain but the membrane C-terminal domain has only two of the fourteen membrane spanning regions. An affinity-purified antipeptide antibody to the novel C-terminus detects an 89 kDa polypeptide which agrees with the molecular mass predicted from the cDNA.
我们从豚鼠柯蒂氏器文库中分离出一个cDNA克隆，它编码阴离子交换蛋白2（AE2）的一种新亚型。该cDNA克隆在编码AE2膜结构域的区域有一个83 bp的缺失。对基因组和cDNA克隆重叠区域的分析表明，缺失部分并不完全对应于一个组成型外显子。产生这种转录本的可变剪接过程涉及内部供体和受体位点，这导致开放阅读框发生移位。产生的多肽具有保守的胞质N端结构域，但膜C端结构域在14个跨膜区域中只有两个。针对新C端的亲和纯化抗肽抗体检测到一条89 kDa的多肽，这与从cDNA预测的分子量一致。
