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[嗜热四膜虫中5个hsp70基因的表达分析]

[Expression analysis of 5 hsp70 genes in Tetrahymena thermophila].

作者信息

Feng Li-Fang, Chang Yue, Yuan Dong-Xia, Miao Wei

机构信息

Key Laboratory of Aquatic Biodiversity and Conservation, Institute of Hydrobiology, the Chinese Academy of Sciences, Wuhan 430072, China.

出版信息

Dongwuxue Yanjiu. 2011 Jun;32(3):267-76. doi: 10.3724/SP.J.1141.2011.03267.

Abstract

Thirteen hsp70 genes with complete conserved domains were identified in Tetrahymena thermophila, and expression of five similar and non-intron hsp70 genes were analyzed. Under heat shock conditions of 37, 39 and 41oC, hsp70-2 mRNA had the highest relative expression level, suggesting it is closely related to heat shock. The basal level of constitutive T. thermophila hsp70-4 gene was high during 20 physiological/developmental stages of growth, starvation and conjugation, and it changed little upon exposure to heat shock: evidence that hsp70-4 is an hsc70 gene. The hsp70-4 cDNA is 2 208 bp long, and contains an open reading frame of 1 959 bp encoding 635 amino acids. Microarray data indicated that T. thermophila hsp70-3 gene probably participated in early starvation (0-12 h) stress and late conjugation (6-10 h) events, such as new macronuclear and micronuclear anlagen formation and old macronuclear elimination. However, hsp70-5 gene possibly participates in late starvation (12-15 h) stress and early conjugation (0-6 h) events such as micronuclear meiosis, micronuclear exchange and pronuclear fusion. Blast2GO indicated that they participated in dissimilar biological processes, suggesting hsp70-3 and hsp70-5 perform different functions.

摘要

在嗜热四膜虫中鉴定出13个具有完整保守结构域的热休克蛋白70(hsp70)基因,并分析了5个相似且无内含子的hsp70基因的表达情况。在37、39和41℃的热休克条件下,hsp70-2 mRNA的相对表达水平最高,表明它与热休克密切相关。组成型嗜热四膜虫hsp70-4基因在20个生长、饥饿和接合的生理/发育阶段的基础水平较高,并且在热休克处理后变化不大:这证明hsp70-4是一个热休克蛋白70同源蛋白(hsc70)基因。hsp70-4 cDNA长2208 bp,包含一个1959 bp的开放阅读框,编码635个氨基酸。微阵列数据表明,嗜热四膜虫hsp70-3基因可能参与早期饥饿(0-12小时)应激和后期接合(6-10小时)事件,如新大核和小核原基的形成以及旧大核的消除。然而,hsp70-5基因可能参与后期饥饿(12-15小时)应激和早期接合(0-6小时)事件,如小核减数分裂、小核交换和原核融合。Blast2GO表明它们参与不同的生物学过程,表明hsp70-3和hsp70-5具有不同的功能。

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