热休克蛋白70 (HSP70)家族成员的生物信息学分析和选择性聚腺苷酸化。

Srishti Shriya, Ramakrushna Paul, Neha Singh, Farhat Afza, Buddhi Prakash Jain
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引用次数: 0

摘要

目的:热休克蛋白70 (HSP70)家族是维持细胞稳态所必需的一组高度保守的分子伴侣。这些蛋白质是蛋白质折叠、组装和降解所必需的,并涉及细胞从应激条件下的恢复。HSP70蛋白在热休克、氧化应激和致病性感染的反应中上调。它们的主要作用是防止蛋白质聚集,重新折叠错误折叠的蛋白质,以及靶向降解不可修复的受损蛋白质。考虑到HSP70蛋白参与基本细胞过程和应激反应,HSP70蛋白对细胞存活和调节癌症、神经退行性疾病和其他病理的疾病结果至关重要。本研究旨在了解不同HSP70成员的结构域结构、物理化学性质、磷酸化、泛素化和替代聚腺苷化位点预测。方法:采用SMART和InterProScan软件进行区域分析。使用EXPASY Protparam、NetPhos 3.1 server DTU和MUbisiDa分别进行理化分析、磷酸化和泛素化位点分析。利用EST数据库研究了选择性聚腺苷酸化。结果:结构域分析表明,在一些HSP70成员中存在螺旋结构域和核苷酸结合结构域。5个HSP70家族成员在其3'UTR中有交替的聚腺苷化位点。结论:本工作对它们的结构、功能、相互作用和聚腺苷化模式提供了有价值的见解。研究它们在癌症等疾病中的治疗潜力可能会有所帮助。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Bioinformatics analysis and alternative polyadenylation in Heat Shock Proteins 70 (HSP70) family members.

Objective: The Heat Shock Protein 70 (HSP70) family is a highly conserved group of molecular chaperones essential for maintaining cellular homeostasis. These proteins are necessary for protein folding, assembly, and degradation and involve cell recovery from stress conditions. HSP70 proteins are upregulated in response to heat shock, oxidative stress, and pathogenic infections. Their primary role is preventing protein aggregation, refolding misfolded proteins, and targeted degradation of irreparably damaged proteins. Given their involvement in fundamental cellular processes and stress responses, HSP70 proteins are critical for cell survival and modulating disease outcomes in cancer, neurodegeneration, and other pathologies. The present study aims to understand domain architecture, physicochemical properties, phosphorylation, ubiquitination, and alternative polyadenylation site prediction in various HSP70 members.

Method: SMART and InterProScan software were used for domain analysis. EXPASY Protparam, NetPhos 3.1 server DTU, and MUbisiDa were used for physicochemical analysis, phosphorylation, and ubiquitination site analysis, respectively. Alternative polyadenylation was studied using the EST database.

Result: Domain analysis shows that coiled-coil and nucleotide-binding domains are present in some of the HSP70 members. Five HSP70 family members have alternate polyadenylation sites in their 3'UTR.

Conclusion: The present work has provided valuable insights into their structure, functions, interactome, and polyadenylation patterns. Studying their therapeutic potential in diseases like cancer can be helpful.

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