Rajapandi Thavamani
Department of Natural Sciences, Science and Technology Center, Coppin State University, 2500 West North Avenue, Baltimore, MD 21216-3698 USA.
J Parasit Dis. 2020 Dec;44(4):687-693. doi: 10.1007/s12639-020-01251-3. Epub 2020 Jul 25.
has the most adenine (A)- and thymine (T)-rich genome known to date, and 24-30% of the proteome contains asparagine (N) and glutamine (Q) residues. In general, asparagine repeats in proteins increase the propensity for aggregation, especially at elevated temperatures, which occur routinely in parasites during exoerythrocytic and erythrocytic developmental stages in a vertebrate host. The exported chaperone machinery is comprised of an exported PfHsp70-x protein and its co-chaperone PfHsp40-x1 in the host erythrocyte compartment, and PfHsp70-z and its co-chaperones in the parasite cytoplasm have been identified. In vitro assays reveal that these chaperone partners function in refolding of asparagine-rich polypeptides. The identification and chaperoning of exported poly-asparagine-containing proteins, and the biological roles and the protection mechanisms of during febrile conditions by the exported chaperone machinery are discussed.
拥有迄今为止已知的腺嘌呤（A）和胸腺嘧啶（T）含量最高的基因组，并且蛋白质组的24 - 30%含有天冬酰胺（N）和谷氨酰胺（Q）残基。一般来说，蛋白质中的天冬酰胺重复序列会增加聚集倾向，尤其是在较高温度下，而在脊椎动物宿主的红细胞外期和红细胞内发育期，寄生虫体内经常会出现较高温度。输出伴侣机制由宿主红细胞区室中的输出型PfHsp70 - x蛋白及其共伴侣PfHsp40 - x1组成，并且已在寄生虫细胞质中鉴定出PfHsp70 - z及其共伴侣。体外试验表明，这些伴侣蛋白对富含天冬酰胺的多肽进行重折叠。本文讨论了输出型含多聚天冬酰胺蛋白的鉴定与陪伴，以及输出伴侣机制在发热条件下的生物学作用和保护机制。
