Hsp-90 and the biology of nematodes.

Hsp-90 and the biology of nematodes.
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DOI:
10.1186/1471-2148-9-254
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发表时间:
2009-10-22
影响因子:
3.4
通讯作者:
Devaney E
Devaney E
中科院分区:
生物学2区
文献类型:
--
作者:
Him NA;Gillan V;Emes RD;Maitland K;Devaney E

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来自自由生活的秀丽隐杆线虫的热蛋白90是独特的,因为它不能结合特异性热蛋白90抑制剂格尔达霉素(GA)。在这里,我们调查了24种不同的自由生活或寄生线虫,目的是确定秀丽隐杆线虫Hsp-90在线虫中是例外还是常态。我们将这些数据与密码子进化模型相结合,试图确定来自ga结合和非ga结合物种的hsp-90是否在不同的进化约束下进化。我们发现GA的结合与生活史有关:自由生活的线虫和那些具有自由生活幼虫期的寄生虫不能结合GA。相比之下,专性寄生虫和那些在环境中自由生活的阶段被封闭在抗性卵内的蠕虫,拥有ga结合的热刺蛋白90。我们分析了15种线虫的Hsp-90序列,以确定线虫的Hsp-90是否经历了影响ga结合的适应性进化。我们的数据提供了hsp-90基因沿着三个独立谱系进化的快速多样化选择的证据,并确定了许多显示适应性进化的重要证据的残基。然而,我们无法证明所观察到的选择是否与结合格尔达霉素的能力相关。Hsp-90是一种多功能蛋白,其基因的快速进化可能与其他关键的细胞功能有关。除初级氨基酸序列外,其他因素也可能影响热休克蛋白90与格尔达霉素结合的能力。
Hsp-90 from the free-living nematode Caenorhabditis elegans is unique in that it fails to bind to the specific Hsp-90 inhibitor, geldanamycin (GA). Here we surveyed 24 different free-living or parasitic nematodes with the aim of determining whether C. elegans Hsp-90 was the exception or the norm amongst the nematodes. We combined these data with codon evolution models in an attempt to identify whether hsp-90 from GA-binding and non-binding species has evolved under different evolutionary constraints. We show that GA-binding is associated with life history: free-living nematodes and those parasitic species with free-living larval stages failed to bind GA. In contrast, obligate parasites and those worms in which the free-living stage in the environment is enclosed within a resistant egg, possess a GA-binding Hsp-90. We analysed Hsp-90 sequences from fifteen nematode species to determine whether nematode hsp-90s have undergone adaptive evolution that influences GA-binding. Our data provide evidence of rapid diversifying selection in the evolution of the hsp-90 gene along three separate lineages, and identified a number of residues showing significant evidence of adaptive evolution. However, we were unable to prove that the selection observed is correlated with the ability to bind geldanamycin or not. Hsp-90 is a multi-functional protein and the rapid evolution of the hsp-90 gene presumably correlates with other key cellular functions. Factors other than primary amino acid sequence may influence the ability of Hsp-90 to bind to geldanamycin.
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