DNAJB3 acts as a cochaperon and stimulates ATPase activity of HSP family genes through its J domain. An in vivo and in silico study was conducted to get comprehensive idea on the role of DNAJB3 gene in goat. The coding sequence of DNAJB3 gene was amplified and searched for polymorphism in three indigenous goat (i.e. Black Bengal, Ganjam and Raighar) populations. One nucleotide substitution at 419th (C > A) position (wild and mutant) with resultant change in amino acid (Ala > Glu) at 140th position was identified. The comparative nucleotide sequence analysis showed 68 variable sites that included 53 parismony informative sites and 15 singleton sites. In silico structural analysis revealed minor difference (7%) in three dimensional protein structure between mutant and wild type DNAJB3 proteins. The protein-protein interactions of DNAJB3 with HSP72, JNK stress kinase, and IKKβ stress kinase were also predicted. The mutant (Raighar) type DNAJB3 protein predicted to interact only with A chain of the JNK stress kinase. Both the wild and mutant type variants of DNAJB3 proteins predicted to interact with A and B chain of hexamer IKKβ stress kinase. This study will be helpful to use DNAJB3 as a molecular marker for thermal tolerance in future.

DNAJB3 作为辅助蛋白，通过其 J 结构域刺激 HSP 家族基因的 ATPase 活性。进行了体内和计算机研究，以全面了解 DNAJB3 基因在山羊中的作用。扩增DNAJB3 基因编码序列并在三个本土山羊（即黑孟加拉、Ganjam 和Raighar）种群中寻找多态性。鉴定了第 419 (C > A) 位置（野生型和突变型）的一个核苷酸取代，导致第 140 位氨基酸（Ala > Glu）发生变化。比较核苷酸序列分析显示 68 个可变位点，其中包括 53 个简约信息位点和 15 个单例位点。电脑模拟结构分析揭示了突变型和野生型 DNAJB3 蛋白质在三维蛋白质结构上的微小差异 (7%)。还预测了 DNAJB3 与 HSP72、JNK 应激激酶和 IKKβ 应激激酶的蛋白质-蛋白质相互作用。突变 (Raighar) 型 DNAJB3 蛋白预测仅与 JNK 应激激酶的 A 链相互作用。DNAJB3 蛋白的野生型和突变型变体均预测与六聚体 IKKβ 应激激酶的 A 和 B 链相互作用。该研究将有助于将来使用DNAJB3作为耐热性的分子标记。