Heat shock protein 70 (Hsp70), a 70-kDa protein, also known as a molecular chaperone, is highly conserved. It plays a major role in cellular functions such as protein folding, regulation of protein degradation, translocation of proteins across membranes, receptor signaling, and protein assembly or disassembly. Vigna radiata is an important legume crop with available whole-genome sequence, but no such study on the HSP70 family is reported. A total of 32 V. radiate HSP70s (Vr-HSP70s) were identified and described. They are phylogenetically clustered into four subgroups. Vr-HSP70s show variations in intron/exon organization. This indicates that introns may play an essential role in gene regulating. The coexpression analysis of Vr-HSP70s revealed that these genes were involved in both abiotic and biotic stresses. Three cytoplasmic hub genes namely Vr-HSP70-C-14, Vr-HSP70-C-29, and Vr-HSP70-C-30 were found common in both stresses. Our findings provide directions for future studies to dissect functional analysis of Vr-HSP70s in response to abiotic and biotic stresses.

中文翻译：

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gna豆中HSP70家族蛋白的全基因组分析以及非生物和生物胁迫下的共表达分析。

热休克蛋白70（Hsp70）是一种70 kDa的蛋白，也被称为分子伴侣，是高度保守的。它在细胞功能中起主要作用，例如蛋白质折叠，蛋白质降解调节，蛋白质跨膜转运，受体信号传导以及蛋白质组装或拆卸。辐射豆（Vigna radiata）是一种重要的豆类作物，具有可用的全基因组序列，但没有关于HSP70家族的此类报道。总辐射32 V鉴定并描述了HSP70s（Vr-HSP70s）。它们在系统发育上分为四个亚组。Vr-HSP70s显示内含子/外显子组织的变异。这表明内含子可能在基因调节中起重要作用。Vr-HSP70s的共表达分析表明，这些基因参与非生物和生物胁迫。发现在这两种胁迫中共有三个胞质中枢基因，即Vr-HSP70-C-14，Vr-HSP70-C-29和Vr-HSP70-C-30。我们的发现为未来研究分析Vr-HSP70s对非生物和生物胁迫的功能提供了方向。