Table of Contents
Molecular Biology International
Volume 2010, Article ID 108429, 7 pages
Research Article

Molecular Characterization of Heat Shock Protein 70-1 Gene of Goat (Capra hircus)

1Division of Physiology and Climatology, Indian Veterinary Research Institute, Izatnagar, Uttar Pradesh, 243 122, India
2Division of Animal Genetics, Indian Veterinary Research Institute, Izatnagar-243 122, Uttar Pradesh, India
3Centre for Wildlife, Indian Veterinary Research Institute, Izatnagar-243 122, Uttar Pradesh, India

Received 28 January 2010; Accepted 14 April 2010

Academic Editor: Sharad S. Singhal

Copyright © 2010 Nitin Gade et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Heat shock protein 70 (HSP 70) plays a vital role by bestowing cytoprotection against diverse kinds of stresses. The ubiquitous HSP 70 proteins are the most abundant and temperature sensitive among all the HSPs. The present paper has characterized HSP70-1 cDNA in goat (Capra hircus). Total RNA isolated from goat peripheral blood mononuclear cells was reverse transcribed to cDNA that was used for amplification of HSP 70-1 gene. PCR product (1926 bp) was cloned in pGEM-T easy vector and sequenced. Sequence analysis revealed 1926-bp-long open reading frame of HSP 70-1 gene encoding 641 amino acids in goat, as reported in cattle. At nucleotide level, goat HSP 70-1 was found to be 96–99% similar to that of sheep (partial), cattle, and buffalo whereas the similarity at amino acid level was 95–100%. Nonsynonymous substitutions exceeding synonymous substitutions indicate the evolution of this protein through positive selection among domestic animals. Goat and sheep appear to have diverged from a common ancestor in phylogenetic analysis. Predicted protein structures of goat HSP 70 protein obtained from deduced amino acid sequence indicated that the functional amino acids involved in chaperoning through ATPase hydrolytic cycle and in uncoating of clathrin coated vesicles are highly conserved.