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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Hsp70-1 from Plasmodium falciparum: protein stability, domain analysis and chaperone activity.
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Hsp70-1 from Plasmodium falciparum: protein stability, domain analysis and chaperone activity.

机译：恶性疟原虫的Hsp70-1：蛋白质稳定性，结构域分析和伴侣活性。

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摘要

P. falciparum contains six copies of the Hsp70 gene of which PfHsp70-1 is important in the parasite's lifecycle. The protein consists of two domains like other Hsp70s but has an unusually long C-terminal tail. The full-length protein is stable towards high temperatures and chemical denaturants. Fluorescence and circular dichroism studies demonstrate that the approximately 42 kDa N-terminalucleotide-binding domain (NBD) is relatively unstable in isolation. Addition of the approximately 35 kDa C-terminal domain with an extended tail containing an EEVD motif confers thermal stability and makes it less susceptible to thermal denaturation. This suggests that the C-terminal domain functions as a stabilization domain. PfHsp70-1 possesses a chaperone activity in addition to other functions reported earlier. We report that the chaperone activity of PfHsp70-1 is enhanced in the presence of P. falciparum Hsp40 (Pfj1, PFD0465w), the homolog of bacterial DnaJ. The present work represents the first evidence for functional interactions between the PfHsp70-1 and Pfj1.
机译：恶性疟原虫含有六个Hsp70基因拷贝，其中PfHsp70-1在寄生虫的生命周期中很重要。该蛋白质与其他Hsp70一样由两个结构域组成，但具有异常长的C末端尾巴。全长蛋白质对高温和化学变性剂稳定。荧光和圆二色性研究表明，大约42 kDa N末端/核苷酸结合域（NBD）在分离中相对不稳定。大约35 kDa的C末端结构域与包含EEVD基序的延伸尾部相结合，赋予了热稳定性，使其不易受到热变性的影响。这表明C末端结构域起稳定结构域的作用。 PfHsp70-1除先前报道的其他功能外，还具有伴侣活性。我们报告说，PfHsp70-1的伴侣活性在恶性疟原虫Hsp40（Pfj1，PFD0465w），细菌DnaJ的同系物的存在下得到增强。本工作代表了PfHsp70-1和Pfj1之间功能相互作用的第一个证据。

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