Computational analyses of amino acid molecules of heat shock protein-70 for elucidating its evolutionary diversity and protein interactions in selected farm animals
Abstract Background The heat shock protein-70 (HSP70) is a protein associated with response and adaptation to stress, as well as protection of the cells against thermal and oxidative stress in animals. It is an evolutionarily conserved protein, but its expression has been reportedly varied. Therefor...
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| Autores principales: | , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
SpringerOpen
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/6d4168facf234c77b67e4417739a3a93 |
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| Sumario: | Abstract Background The heat shock protein-70 (HSP70) is a protein associated with response and adaptation to stress, as well as protection of the cells against thermal and oxidative stress in animals. It is an evolutionarily conserved protein, but its expression has been reportedly varied. Therefore, this study implemented computational analyses of the amino acid sequences of this gene for a better understanding of the evolutionary and protein interactions variations associated with the gene to facilitate its exploitation for the breeding of animals with increasing adaptation to heat stress. Results The result showed that there is a wide evolutionary distance between humans and the selected farm animals studied but elegans shared a common evolutionary relationship with the farm animals. The sequence identity analysis returned exact matches among the sequences as minimum = 8.09%, maximum = 98.58%, and mean ± SD = 71.03 ± 26.3% across all the species, while the sequence similarities resemblance among the sequences were minimum = 16.49%, maximum = 100%, and mean ± SD = 78.99 ± 24.39%. The global block substitution matrix (BLOSUM62) analysis returned minimum = 0.18, maximum = 0.98, and mean ± SD = 0.62 ± 0.34. The analysis of the molecular weight of the protein sequences returned minimum = 5.70 kDa, maximum = 6.41 kDa, mean = 6.28 kDa, and standard deviation 0.17 kDa, and the isoelectric point of the protein sequences was minimum = 4.55, maximum = 7.17, mean = 5.56, and standard deviation = 0.65 while the hydrophobicity of the protein sequences were minimum = 45.20 kcal/mol, maximum = 53.02 kcal/mol, mean = 47.81 kcal/mol, and standard deviation = 1.85 kcal/mol. Conclusion The outcomes of the computational analyses led to the conclusion that variations exist in the conservations of amino acid residues of the gene in the studied farm and non-farm animals, and this is responsible for the differences and similarities in the expression of the HSP70 gene in different animals. It was also concluded that elegans are suitable model that could be exploited for a better understanding of response and adaptation to heat stress in duck, chicken, cattle, sheep, and goat when focusing on regulation and expression of heat shock protein gene 70 (HSP70). |
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