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首页> 外文期刊>Molecular and Cellular Biology >Alternative primary structures in the transmembrane domain of the chicken erythroid anion transporter.
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Alternative primary structures in the transmembrane domain of the chicken erythroid anion transporter.

机译：鸡类红系阴离子转运蛋白跨膜结构域的替代一级结构。

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Isolation and characterization of the chicken erythroid anion transporter (band 3) cDNA clone, pCHB3-1, revealed that the chicken erythroid band 3 polypeptide is 844 amino acids in length with a predicted mass of 109,000 daltons. This polypeptide is composed of a hydrophilic N-terminal cytoplasmic domain and a hydrophobic C-terminal transmembrane domain. The approximately 90 N-terminal amino acids of the human and murine erythroid band 3 polypeptides are absent in the predicted sequence of the chicken erythroid band 3 polypeptide. The absence of this very acidic N-terminal region is consistent with the lack of binding of glyceraldehyde-3-phosphate dehydrogenase to chicken erythroid band 3, as well as the relatively basic isoelectric point observed for this molecule. The remainder of the cytoplasmic domain shows little similarity to the cytoplasmic domain of the murine and human erythroid band 3, with the exception of the putative ankyrin-binding site, which is highly conserved. In contrast, the transmembrane domain of the chicken band 3 polypeptide is very similar to that of the murine erythroid and human nonerythroid band 3 polypeptides. The transmembrane domain contains 10 hydrophobic regions that could potentially traverse the membrane 12 to 14 times. In addition, a variant of chicken erythroid band 3, pCHB3-2, was cloned in which one of the hydrophobic regions of pCHB3-1 is lacking. The transcript complementary to pCHB3-2 accumulated in chicken erythroid cells in a similar manner as the transcript complementary to pCHB3-1 during embryonic development. This is the first example of a transporter protein or ion channel with alternative primary structures in its membrane-spanning segments.
机译：鸡红系阴离子转运蛋白（带3）cDNA克隆pCHB3-1的分离和鉴定显示，鸡红系带3多肽的长度为844个氨基酸，预计质量为109,000道尔顿。该多肽由亲水的N端细胞质结构域和疏水的C端跨膜结构域组成。人和鼠类红系带3多肽的约90个N末端氨基酸不在鸡类红系带3多肽的预测序列中。该极酸性的N-末端区域的缺乏与甘油醛-3-磷酸脱氢酶与鸡红系带3的结合缺乏以及对该分子观察到的相对碱性的等电点一致。胞质结构域的其余部分与鼠和人红系带3的胞质结构域几乎没有相似性，只是假定的锚蛋白结合位点高度保守。相反，鸡条带3多肽的跨膜结构域与鼠类红细胞和人非红系带3多肽的跨膜结构域非常相似。跨膜结构域包含10个疏水区域，这些区域可能会穿过膜12到14次。另外，克隆了鸡红系带3的变体pCHB3-2，其中缺少pCHB3-1的疏水区域之一。与pCHB3-2互补的转录物以与胚胎发育过程中与pCHB3-1互补的转录物相似的方式积累在鸡类红细胞中。这是转运蛋白或离子通道在其跨膜区段中具有替代一级结构的第一个例子。

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