Elucidation of Diverse Physico-Chemical Parameters in Mammalian Small Heat Shock Proteins: A Comprehensive Classification and Structural and Functional Exploration Using In Silico Approach
| Autor: | Angshuman Bagchi, Rakhi Dasgupta, Sangeeta Mitra |
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| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
Pan troglodytes Cellular differentiation In silico Cell Bioengineering 01 natural sciences Applied Microbiology and Biotechnology Biochemistry Protein Structure Secondary Mice Dogs 010608 biotechnology medicine Animals Humans Computer Simulation Phosphorylation Molecular Biology Small Heat-Shock Proteins Protein secondary structure Multiple sequence alignment biology 010405 organic chemistry General Medicine Macaca mulatta 0104 chemical sciences Cell biology Heat-Shock Proteins Small medicine.anatomical_structure Organ Specificity Chaperone (protein) biology.protein Cattle Biotechnology |
| Zdroj: | Applied biochemistry and biotechnology. 193(6) |
| ISSN: | 1559-0291 |
| Popis: | Small heat shock proteins (sHSPs), often known as molecular chaperones, are most prevalent in nature. Under certain stress-induced conditions, these sHSPs act as an ATP-independent variation and thus prevent the inactivation of various non-native substrate proteins and their aggregation. They also assist other ATP-dependent chaperones in the refolding of these substrates. In the case of prokaryotes and lower eukaryotes, the chaperone functions of sHSPs can bind a wide range of cellular proteins but preferentially protect translation-related proteins and metabolic enzymes. Eukaryotes usually encode a larger number of sHSPs than those of prokaryotes. The chaperone functions of mammalian sHSPs are regulated by phosphorylation in cells and also by temperature. Their sHSPs have different sub-cellular compartments and cell/tissue specificity. The substrate proteins of mammalian sHSPs or eukaryotic sHSPs accordingly reflect their multi-cellular complexity. The sHSPs of animals play roles in different physiological processes as cell differentiation, apoptosis, and longevity. In this work, the characterization, location, tissue specificity, and functional diversity of sHSPs from seven different mammalian species with special emphasis on humans have been studied. Through this extensive work, a novel and significant attempt have been made to classify them based on their omnipresence, tissue specificity, localization, secondary structure, probable mutations, and evolutionary significance. |
| Databáze: | OpenAIRE |
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