Genomic insulin is located on the short arm of chromosome 11 in human genome. It is a well studied polypeptide hormone, consists of 110 amino acids which start with signaling peptide of 1-24 amino acids, B-chain of 25-54 amino acids, C-peptide of 55-89 amino acids and end with A-chain of 90-110 amino acids. Insulin, produced by the beta cell of the pancreas in response to glucose stimuli, binds to its receptor rapidly due to receptor autophosphorylation and primordially regulates nutritional metabolic pathways. In this study we have depicted and explored evolutionary conservation rate, insight into structure and phylogenetic connection of insulin molecule among eight mammalian species; Homo sapiens (Human), Bos taurus (Cattle), Cavia porcellus (Guinea pig), Canis lupus familiaris (Dog), Gorilla gorilla (Western gorilla), Ovis aries (Sheep), Pan troglodytes (Chimpanzee), Pongo pygmaeus (Orangutan) using Computational Biology. The analysis of physico-chemical characteristics, secondary and 3-D structure prediction of insulin in different species identified phylogenetically most related species. The major findings are that genomic insulin from Human and Dog has a lowest genetic distance of 0.13 of the mammalian species studied. Human and Guinea pig has the next lowest genetic distance of 0.39 and 69.1% identical at the amino acid level. Whereas Human and Western gorilla has genetic distances of 0.00 and 100% identical at the amino acid level and share a common node on the phylogenetic tree. Physico-chemical study also shows that these sequences show high leucine content (18.2%) with high instability index (>40) except Sheep and Cattle has low leucine and instability index (<40). The sequence analysis among species has allowed us to know the manner in which the insulin has evolved over million–year period. This study result provides rapid comprehensive information to calculate the amino acid sequences in relations to evolutionary conservation rates as well as molecular phylogenetics.
| Published in | Ecology and Evolutionary Biology (Volume 1, Issue 2) |
| DOI | 10.11648/j.eeb.20160102.13 |
| Page(s) | 23-28 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2016. Published by Science Publishing Group |
Molecular Phylogenetics, Genomic Insulin, Multiple Sequence Alignment, Pairwise Distances, Physico-chemical Characteristics, Secondary Structure, 3D Structure Prediction
| [1] | Suzanne E. McGaugh, Anne M. Bronikowski, Chih-HorngKuo et al.,(2015). ‘‘Rapid molecular evolution across amniotes of the IIS/TOR network,’’ Proc Natl Acad Sci U S A. 112 (22):7055-7060. |
| [2] | De Souza AM, Lopez JA, (2004). ‘‘Insulin or insulin-like studies on unicellular organism: a review,’’ Barzarch. Boil. Technol. 47 (60). |
| [3] | Steiner D, N. Fox, S. Smeekens, S. Ohagi, G. Westermark, and S. Chan, (1993). ‘‘Newmolecular perspectives in islet hormone biosynthesis,’’Biochem. Soc. Trans. 21:139–142. |
| [4] | Shu Jin Chan and Donald F. Steiner, (2000). ‘‘Insulin Through the Ages: Phylogeny of Growth Promoting and Metabolic Regulatory Hormone,’’ Amer. Zoo L. 40: 213-222. |
| [5] | Kearse M, Moir R, Wilson A et al., (2012). ‘‘Geneious Basic: an integrated and extendable desktop software platform for the organization and analysis of sequence data,’’ Bioinformatices, 28 (12): 1647-9. |
| [6] | Tamura K., Peterson D, Peterson N, Stecher G, Nei M, and Kumar S, (2011). ‘‘MEGA5: Molecular Evolutionary Genetics Analysis using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony Methods,’’ Molecular Biology and Evolution 28: 2731-2739. |
| [7] | Lukasz k, RazibAa, Aghakhani S, Dick S, Mizianty M, Jahandibeh S, (2009). ‘‘CRYSTALP2: sequences-based protein crystallization propensity prediction,’’ BMC structural Biology 9:50. |
| [8] | Geourjon C, Deleage G, (1995). ‘‘SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments,’’Comput Appl Biosci; 11 [6]: 681-84. |
| [9] | Bates PA, Kelly LA, Mac Callum RM, Sternberg MJE (2001). ‘‘Enhancement of Protein Modelling by Human Intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM.’’Proteins: Structure, Function and Genetics, Suppl5: 39-46. |
| [10] | Jones D.T, Taylor W.R, and Thornton J.M, (1992). ‘‘The rapid generation of mutation data matrices from protein sequences,’’ Computer Applications in the Biosciences 8: 275-282. |
| [11] | http://web.expasy.org/docs/expasy_tools05.pdf. |
| [12] | Zuckerkandl E. and Pauling L, (1965). ‘‘Evolutionary divergence and convergence in proteins. Edited in Evolving Genes and Proteins by V. Bryson and H.J. Vogel, pp. 97-166. Academic Press, New York. |
APA Style
M. A Hashem, Neena Islam, Md. Moinul Abedin Shuvo, Md. Arifuzzaman. (2016). Evolutionary Relationship of Genomic Insulin Sequence in Different Mammalian Species: A Computational Approach. Ecology and Evolutionary Biology, 1(2), 23-28. https://doi.org/10.11648/j.eeb.20160102.13
ACS Style
M. A Hashem; Neena Islam; Md. Moinul Abedin Shuvo; Md. Arifuzzaman. Evolutionary Relationship of Genomic Insulin Sequence in Different Mammalian Species: A Computational Approach. Ecol. Evol. Biol. 2016, 1(2), 23-28. doi: 10.11648/j.eeb.20160102.13
Share This Article
Twitter
Linked In
Facebook
Copy
Download@article{10.11648/j.eeb.20160102.13,
author = {M. A Hashem and Neena Islam and Md. Moinul Abedin Shuvo and Md. Arifuzzaman},
title = {Evolutionary Relationship of Genomic Insulin Sequence in Different Mammalian Species: A Computational Approach},
journal = {Ecology and Evolutionary Biology},
volume = {1},
number = {2},
pages = {23-28},
doi = {10.11648/j.eeb.20160102.13},
url = {https://doi.org/10.11648/j.eeb.20160102.13},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.eeb.20160102.13},
abstract = {Genomic insulin is located on the short arm of chromosome 11 in human genome. It is a well studied polypeptide hormone, consists of 110 amino acids which start with signaling peptide of 1-24 amino acids, B-chain of 25-54 amino acids, C-peptide of 55-89 amino acids and end with A-chain of 90-110 amino acids. Insulin, produced by the beta cell of the pancreas in response to glucose stimuli, binds to its receptor rapidly due to receptor autophosphorylation and primordially regulates nutritional metabolic pathways. In this study we have depicted and explored evolutionary conservation rate, insight into structure and phylogenetic connection of insulin molecule among eight mammalian species; Homo sapiens (Human), Bos taurus (Cattle), Cavia porcellus (Guinea pig), Canis lupus familiaris (Dog), Gorilla gorilla (Western gorilla), Ovis aries (Sheep), Pan troglodytes (Chimpanzee), Pongo pygmaeus (Orangutan) using Computational Biology. The analysis of physico-chemical characteristics, secondary and 3-D structure prediction of insulin in different species identified phylogenetically most related species. The major findings are that genomic insulin from Human and Dog has a lowest genetic distance of 0.13 of the mammalian species studied. Human and Guinea pig has the next lowest genetic distance of 0.39 and 69.1% identical at the amino acid level. Whereas Human and Western gorilla has genetic distances of 0.00 and 100% identical at the amino acid level and share a common node on the phylogenetic tree. Physico-chemical study also shows that these sequences show high leucine content (18.2%) with high instability index (>40) except Sheep and Cattle has low leucine and instability index (<40). The sequence analysis among species has allowed us to know the manner in which the insulin has evolved over million–year period. This study result provides rapid comprehensive information to calculate the amino acid sequences in relations to evolutionary conservation rates as well as molecular phylogenetics.},
year = {2016}
}
TY - JOUR T1 - Evolutionary Relationship of Genomic Insulin Sequence in Different Mammalian Species: A Computational Approach AU - M. A Hashem AU - Neena Islam AU - Md. Moinul Abedin Shuvo AU - Md. Arifuzzaman Y1 - 2016/09/22 PY - 2016 N1 - https://doi.org/10.11648/j.eeb.20160102.13 DO - 10.11648/j.eeb.20160102.13 T2 - Ecology and Evolutionary Biology JF - Ecology and Evolutionary Biology JO - Ecology and Evolutionary Biology SP - 23 EP - 28 PB - Science Publishing Group SN - 2575-3762 UR - https://doi.org/10.11648/j.eeb.20160102.13 AB - Genomic insulin is located on the short arm of chromosome 11 in human genome. It is a well studied polypeptide hormone, consists of 110 amino acids which start with signaling peptide of 1-24 amino acids, B-chain of 25-54 amino acids, C-peptide of 55-89 amino acids and end with A-chain of 90-110 amino acids. Insulin, produced by the beta cell of the pancreas in response to glucose stimuli, binds to its receptor rapidly due to receptor autophosphorylation and primordially regulates nutritional metabolic pathways. In this study we have depicted and explored evolutionary conservation rate, insight into structure and phylogenetic connection of insulin molecule among eight mammalian species; Homo sapiens (Human), Bos taurus (Cattle), Cavia porcellus (Guinea pig), Canis lupus familiaris (Dog), Gorilla gorilla (Western gorilla), Ovis aries (Sheep), Pan troglodytes (Chimpanzee), Pongo pygmaeus (Orangutan) using Computational Biology. The analysis of physico-chemical characteristics, secondary and 3-D structure prediction of insulin in different species identified phylogenetically most related species. The major findings are that genomic insulin from Human and Dog has a lowest genetic distance of 0.13 of the mammalian species studied. Human and Guinea pig has the next lowest genetic distance of 0.39 and 69.1% identical at the amino acid level. Whereas Human and Western gorilla has genetic distances of 0.00 and 100% identical at the amino acid level and share a common node on the phylogenetic tree. Physico-chemical study also shows that these sequences show high leucine content (18.2%) with high instability index (>40) except Sheep and Cattle has low leucine and instability index (<40). The sequence analysis among species has allowed us to know the manner in which the insulin has evolved over million–year period. This study result provides rapid comprehensive information to calculate the amino acid sequences in relations to evolutionary conservation rates as well as molecular phylogenetics. VL - 1 IS - 2 ER -
Email: