黏结蛋白的功能活性可被化学伴侣改变。

IF 1.4 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Sayali Marathe, Haripriya Chougule, Vandana Nikam, Amitabha Majumdar, Tania Bose
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引用次数: 0

摘要

内聚蛋白复合物在染色体分离、转录、DNA复制和染色体凝聚等过程中起着非常重要的作用。内聚蛋白的突变引起一种统称为内聚蛋白病的疾病。黏结病的主要原因是由于与基因表达相关的缺陷,从而引起发育障碍。我们使用酿酒酵母模拟了具有与人类(esco2)同源突变(eco1W216G)的黏结性疾病罗伯茨综合征。我们的数据表明,像山梨醇这样的多元醇糖可以修复错误折叠的蛋白质,减少内质网和蛋白质静态应激。我们使用山梨糖醇作为化学伴侣,来检查它如何恢复Roberts表型内聚蛋白突变体的染色体分离、基因表达、错误调控、蛋白质错误折叠、自噬和翻译缺陷。分子对接帮助我们确定了Eco1上可能改变表型性状的位点。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Functional Activities of Cohesin Proteins Can Be Altered by Chemical Chaperones

Functional Activities of Cohesin Proteins Can Be Altered by Chemical Chaperones

The cohesin protein complex plays a very important role in chromosome segregation, transcription, DNA replication and chromosome condensation. Mutations in cohesin proteins give rise to a disease collectively referred to as Cohesinopathies. The major cause of cohesinopathies arise due to defects associated with gene expression, that give rise to developmental disorders. We have used Saccharomyces cerevisiae to mimic the cohesinopathy disorder Roberts syndrome with mutations (eco1W216G) homologous to that of humans (esco2). Our data suggests that polyol sugars like sorbitol, can repair misfolded proteins and reduce ER and proteostatic stress. We have used sorbitol as a chemical chaperone, to check how it can restore chromosome segregation, gene expression, misregulation, protein misfolding, autophagy and translational defects in the cohesin mutant of the Roberts’ phenotype. Molecular docking has helped us identify the possible sites on Eco1, which could possibly alter the phenotypic traits.

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来源期刊
The Protein Journal
The Protein Journal 生物-生化与分子生物学
CiteScore
5.20
自引率
0.00%
发文量
57
审稿时长
12 months
期刊介绍: The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.
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