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首页> 外文期刊>Molecular and Cellular Biology >Novel N-terminal amino acid sequence required for retention of a hepatitis B virus glycoprotein in the endoplasmic reticulum.
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Novel N-terminal amino acid sequence required for retention of a hepatitis B virus glycoprotein in the endoplasmic reticulum.

机译：乙型肝炎病毒糖蛋白保留在内质网中所需的新的N末端氨基酸序列。

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摘要

The preS1 surface glycoprotein of hepatitis B virus is targeted to the endoplasmic reticulum (ER) and is retained in this organelle when expressed in the absence of other viral gene products. The protein is also acylated at its N terminus with myristic acid. Sequences responsible for its ER retention have been identified through examination of mutants bearing lesions in the preS1 coding region. These studies reveal that such sequences map to the N terminus of the molecule, between residues 6 and 19. Molecules in which this region was present remained in the ER; those in which it had been deleted were secreted from the cell. Although all deletions which allowed efficient secretion also impaired acylation of the polypeptide, myristylation alone was not sufficient for ER retention: point mutations which eliminated myristylation did not lead to secretion. These data indicate that an essential element for ER retention resides in a 14-amino-acid sequence that is unrelated to previously described ER retention signals.
机译：乙型肝炎病毒的preS1表面糖蛋白靶向内质网（ER），并且在不存在其他病毒基因产物的情况下表达时保留在该细胞器中。该蛋白质还在其N末端被肉豆蔻酸酰化。通过检查在preS1编码区中带有损伤的突变体，已经鉴定了导致其ER保留的序列。这些研究表明，这些序列映射到分子的N末端，残基6和19之间。存在该区域的分子仍保留在ER中。那些已经被删除的细胞从细胞中分泌出来。尽管所有允许有效分泌的缺失都损害了多肽的酰化作用，但仅肉豆蔻化不足以保留ER：消除肉豆蔻化的点突变不会导致分泌。这些数据表明，用于ER保留的必要元件存在于与先前描述的ER保留信号无关的14个氨基酸的序列中。

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