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首页> 外文OA文献 >Aberrant membrane insertion of a cytoplasmic tail deletion mutant of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.
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Aberrant membrane insertion of a cytoplasmic tail deletion mutant of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.

机译：新城疫病毒血凝素神经氨酸酶糖蛋白胞质尾缺失突变体的异常膜插入。

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摘要

The hemagglutinin-neuraminidase (HN) protein of Newcastle disease virus (NDV) is a type II glycoprotein oriented in the plasma membrane with its amino terminus in the cytoplasm and its carboxy terminus external to the cell. We have previously shown that the membrane insertion of HN protein requires signal recognition particle SRP, occurs cotranslationally, and utilizes the same GTP-dependent step that has been described for secretory proteins, type I proteins, and multispanning proteins (C. Wilson, R. Gilmore, and T. Morrison, Mol. Cell. Biol. 7:1386-1392, 1987; C. Wilson, T. Connolly, T. Morrison, and R. Gilmore, J. Cell Biol. 107:69-77, 1988). The role of the amino-terminal cytoplasmic domain in the faithful membrane insertion of this type II protein was explored by characterizing the membrane integration of a mutant lacking 23 of the 26 amino acids of the cytoplasmic domain. The mutant protein was able to interact with SRP, resulting in translation inhibition, membrane targeting, and membrane translocation, but the efficiency of translocation was considerably lower than for the wild-type HN protein. In addition, a significant proportion of the mutant protein synthesized in the presence of SRP and microsomal membranes was associated with the membrane in an EDTA- and alkali-insensitive manner yet integrated into membranes with its carboxy-terminal domain on the cytoplasmic side of membrane vesicles. Membrane-integrated molecules with this reverse orientation were not detected when the mutant protein was synthesized in the absence of SRP or a functional SRP receptor. Truncated mRNAs encoding amino-terminal segments of the wild-type and mutant proteins were translated to prepare ribosomes bearing arrested nascent chains. The arrested mutant nascent chain, in contrast to the wild-type nascent chain, was also able to insert into membranes in a GTP- and SRP-independent manner. Results suggest that the cytoplasmic domain plays a role in the proper membrane insertion of this type II glycoprotein.
机译：新城疫病毒（NDV）的血凝素神经氨酸酶（HN）蛋白是一种定向于质膜的II型糖蛋白，其氨基端在细胞质中，而羧基端在细胞外。先前我们已经证明，HN蛋白的膜插入需要信号识别颗粒SRP，共翻译发生，并利用与分泌蛋白，I型蛋白和多跨度蛋白相同的GTP依赖性步骤（C.Wilson，R. Gilmore and T.Morrison，Mol.Cell.Biol.7：1386-1392，1987; C.Wilson，T.Connolly，T.Morrison和R.Gilmore，J.Cell Biol.107：69-77，1988 ）。通过表征缺少胞质结构域的26个氨基酸中的23个的突变体的膜整合，探索了氨基末端胞质结构域在II型蛋白质的忠实膜插入中的作用。突变蛋白能够与SRP相互作用，导致翻译抑制，膜靶向和膜易位，但易位效率明显低于野生型HN蛋白。此外，在SRP和微粒体膜存在下合成的大量突变蛋白以EDTA和碱不敏感的方式与膜结合，但整合到膜中，其羧基末端结构域位于膜囊泡的细胞质侧。当在没有SRP或功能性SRP受体的情况下合成突变蛋白时，未检测到具有这种反向取向的膜整合分子。翻译编码野生型和突变蛋白的氨基末端片段的截短的mRNA，以制备携带被捕新生链的核糖体。与野生型新生链相反，被捕获的突变新生链也能够以不依赖GTP和SRP的方式插入膜中。结果表明，胞质结构域在该II型糖蛋白的适当膜插入中起作用。

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