Use of Bioinformatics Tools to Study Myostatin Protein

Document Type : research

Authors

1 Ph.D. Student, Department of Nano Biotechnology, Faculty of Life Science, Tarbiat Modares University, Tehran, Tehran

2 M.Sc. Graduate, Department of Biotechnology, Faculty of Agriculture, Shahed University of Tehran, Tehran

3 Assistant Professor, Biology Department, Faculty of Science, Islamic Azad University of Shiraz, Shiraz

4 Department of Agriculture, Payame Noor University, Tehran

Abstract

Myostatin gene belongs to the family of transforming growth factors (TGF-β), which in growth and development and maturation and specifically is expressed in adult skeletal muscle development. In this study protein amino acid sequence of Myostatin in various species, including cow, sheep, goats, horses, pigs, chickens, turkeys, ducks, goose, Columba, rats, and humans was investigated using by Bioinformatics tools. In alignment of the final section of Myostatin protein (active form of Myostatin protein that is expressed as a dimer), high degree of conservation was observed, so that the changes fluctuation in this section than the other parts of protein sequence, the least amount possible. Secondary structures such as alpha helices, beta sheets and three-dimensional structure of Myostatin proteins using specialized sites Proteus and Phyre2 was assessed. Amino acids leucine, lysine, isoleucine and glutamic acid in cow, sheep and goat showed the same frequency as compared with poultry, such as chicken, lots more. However, the frequency of the amino acid sequence of the protein myostatin in humans and pigs was moderate. Study of phylogenetic tree showed that difference between amino acid sequences among mentioned Myostatin species lead exposure in a group of birds was isolated from mammals. Investigation of 3-D structure showed that this gene is highly conserved across species.

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References

Bellinge, R. H. S., Liberles, D. A., Laschi, S. P. A. O., Brien, P. A. and Tay, G. K. 2004. Myostatin and its implications on animal breeding: a review. International Society for Animal Genetics Animal Genetics, 36: 1-6.
Cassar-Malek, I., Passelaigue, F., Bernard, C., Jean, L. and Hocquette, J. F. 2007. Target genes of myostatin loss-of-function in muscles of late bovine fetuses. BMC Genomics, 8: 63.
Hadizadeh, M., Mohammadabadi, M., Niazi, A., Esmailizadeh, A., Mehdizadeh, Y. and Mollaei, A. 2013. Bioinformatics analysis of the GDF9 exon 2 in Tali and Beetal goats. Modern Genetics Journal, 3: 283-288.
Joulia-Ekaza, D. and Cabello, G. 2006. Myostatin regulation of muscle development: Molecular basis, natural mutations, physiological aspects. Experimental Cell Research, 312: 2401-14.
Khani, K., Abdolmohammadi, A., Foroutanifar, S. and Zebarjadi, A. 2014. Association of polymorphism in 5`UTR and exon1 regions of myostatin gene with twining trait in markhoz goat breed. Genetics in the 3rd Millennium Journal, 2: 3536-35543.
Malboobi, M., Feyzi, A. and Lohrasebi, T. 2010. Practical Guide to Data Processing of Biology and Genome Projects. pp. 113-115
Miar, Y., Salehi, A. R., AleYasin, S. A. and Raoufzadeh, S. 2011. Study of polymorphism in myostatin gene in Chaal, Zel and Zandi Iranian sheep breeds. Journal of Animal Production, 13: 33-40.
Mousavi-Movahedi, A., Jamni, A., Taghvi, A. and Moghadamnia, S. A. 2009. Proteins structure and function. Tehran University Press, Tehran, Iran. Page 202.
Nelson, D. L. and Cox, M. M. 2008. Principles of Biochemestry. 160 pp.
Soufy, B., Mohammadabadi, M. R., Shojaiyan, K., Baghizadeh, A., Farasaty, S., Askari, N. and Dayani, O. 2009. Evaluation of myostatin gene polymorphism in sanjabi sheep by PCR-RFLP. Journal of Animal Science Researches, 19: 81-90.
Thomas, M., Langley, B., Berry, C., Sharma, M., Kirk, S., Bass, J. and Kambadur, R. 2000. Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation. Journal of Biological Chemistry, 275: 40235-40243.
Uytterhaegen, L., Claeys, E. and Demeyer, D. 1994. Effects of exogenous protease effectors on beef tenderness development and myofibrillar degradation and solubility. Journal of Animal Science, 72: 1209-23.
Volume 6, Issue 2
May 2016
Pages 45-49

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