Transcriptional regulation of heat shock protein 70 genes by class I histone deacetylases in the red flour beetle, Tribolium castaneum.,Insect Molecular Biology

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Transcriptional regulation of heat shock protein 70 genes by class I histone deacetylases in the red flour beetle, Tribolium castaneum.
Insect Molecular Biology ( IF 2.3 ) Pub Date : 2019-12-10 , DOI: 10.1111/imb.12627
M Chen ₁ , N Zhang ₁ , H Jiang ₁ , X Meng ₁ , K Qiang ₁ , J Wang _{1,

2}

Affiliation

The regulatory function of histone acetylation in the expression of genes encoding heat shock proteins (Hsps) has been documented in Drosophila melanogaster; however, knowledge of the role of acetylation in modulating Hsps in other insect pests is limited. In this study, two full‐length cDNAs encoding inducible Hsp70 (designated TcHsp70) and heat shock cognate 70 (TcHsc70) were isolated and characterized in the red flour beetle, Tribolium castaneum. TcHsp70 and TcHsc70 cDNAs were 2256 and 2132 bp and encoded 1941‐ and 1893‐bp open reading frames, respectively. The deduced TcHsp70 and TcHsc70 proteins contained 646 and 630 amino acids, respectively, and contained sequences typical of the Hsp70 family, including the EEVD motif for cytoplasmic localization. Expression patterns after heat shock indicated that TcHsp70 was strongly heat‐inducible, whereas the expression level of TcHsc70 remained unchanged under heat shock. RNA interference‐mediated knock‐down of three genes encoding class I histone deacetylases differentially influenced both basal and heat shock inducible expression of TcHsp70 and TcHsc70, suggesting the involvement of histone acetylation in epigenetic regulation of Hsp70 transcription in T. castaneum.

中文翻译：

红皮甲虫Tribolium castaneum中I类组蛋白脱乙酰基酶对热休克蛋白70基因的转录调控。

在果蝇中已经证明了组蛋白乙酰化在编码热激蛋白（Hsps）的基因表达中的调节功能。但是，关于乙酰化在其他害虫中调控Hsps的作用的知识是有限的。在这项研究中，分离了编码全长Hsp70（命名为TcHsp70）和热休克同源蛋白70（TcHsc70）的两个全长cDNA，并在红色面粉甲虫Tribolium castaneum中进行了鉴定。TcHsp70和TcHsc70cDNAs为2256和2132 bp，分别编码1941和1893 bp开放阅读框。推导的TcHsp70和TcHsc70蛋白分别包含646和630个氨基酸，并包含Hsp70家族的典型序列，包括用于细胞质定位的EEVD基序。热激后的表达模式表明TcHsp70具有很强的热诱导性，而TcHsc70的表达水平在热激后保持不变。RNA干扰介导的编码I类组蛋白脱乙酰基酶的三个基因的敲除差异影响TcHsp70和TcHsc70的基础和热休克诱导表达，提示组蛋白乙酰化参与Hsp70的表观遗传调控cast树转录。

更新日期：2019-12-10

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