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硕大利什曼原虫:一种细胞质应激相关蛋白的特性与表达

Leishmania major: characterisation and expression of a cytoplasmic stress-related protein.

作者信息

Searle S, Smith D F

机构信息

Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, U.K.

出版信息

Exp Parasitol. 1993 Aug;77(1):43-52. doi: 10.1006/expr.1993.1059.

DOI:10.1006/expr.1993.1059
PMID:7916697
Abstract

The DNA sequence of a single-copy gene from Leishmania major has been determined and shown to share sequence identity with eukaryotic heat shock protein-70-related genes. Conserved features of the deduced open reading frame include amino acids implicated in ATP binding and a putative calmodulin-binding domain. Antibodies generated to the recombinant fusion protein recognise a 70-kDa molecule of pI 6.0. This molecule is constitutively expressed and localises to the cytoplasm in all stages of the parasite life cycle.

摘要

已经确定了来自硕大利什曼原虫的一个单拷贝基因的DNA序列,并显示其与真核热休克蛋白-70相关基因具有序列同一性。推导的开放阅读框的保守特征包括与ATP结合有关的氨基酸和一个假定的钙调蛋白结合结构域。针对重组融合蛋白产生的抗体识别出一个分子量为70 kDa、等电点为6.0的分子。该分子组成性表达,并定位于寄生虫生命周期所有阶段的细胞质中。

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Heat shock causes a decrease in polysomes and the appearance of stress granules in trypanosomes independently of eIF2(alpha) phosphorylation at Thr169.热休克会导致锥虫中多核糖体减少,并出现应激颗粒,这一过程与eIF2(α)在苏氨酸169位点的磷酸化无关。
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