Format

Send to

Choose Destination
Int J Biol Macromol. 2015 Nov;81:195-204. doi: 10.1016/j.ijbiomac.2015.07.058. Epub 2015 Jul 31.

The Arabian camel Camelus dromedarius heat shock protein 90α: cDNA cloning, characterization and expression.

Author information

1
Department of Biotechnology, Institute of Graduate Studies and Research, Alexandria University, Alexandria, Egypt. Electronic address: hesham25166@hotmail.com.
2
Genetic Engineering and Biotechnology Research Institute (GEBRI), City for Scientific Research and Technology Applications, Alexandria, Egypt.
3
Department of Biotechnology, Institute of Graduate Studies and Research, Alexandria University, Alexandria, Egypt.
4
Biochemistry Department, College of Science King Saud University, Bld. 5, Lab AA10, P.O. Box 2454, Riyadh, Saudi Arabia.
5
Biochemistry Department, College of Science King Saud University, Bld. 5, Lab AA10, P.O. Box 2454, Riyadh, Saudi Arabia; Integrated Gulf Biosystems, Riyadh 11391, Saudi Arabia.
6
Biochemistry Department, College of Science King Saud University, Bld. 5, Lab AA10, P.O. Box 2454, Riyadh, Saudi Arabia; National Research Centre, 33 El-Bohouth St. (Former El-Tahrir St.), P.O. 12622, Dokki, Giza, Egypt.
7
Molecular Biology Department, Genetic Engineering and Biotechnology Institute, University of Sadat City, Egypt.

Abstract

Heat shock protein 90 (Hsp90) is a highly conserved ubiquitous molecular chaperone contributing to assisting folding, maintenance of structural integrity and proper regulation of a subset of cytosolic proteins. In the present study, a heat shock protein 90α full length coding cDNA was isolated and cloned from the Arabian one-humped camel by reverse transcription polymerase chain reaction (RT-PCR). The full length cDNA sequence was submitted to NCBI GeneBank under the accession number KF612338. The sequence analysis of the Arabian camel Hsp90α cDNA showed 2202bp encoding a protein of 733 amino acids with estimated molecular mass of 84.827kDa and theoretical isoelectric point (pI) of 5.31. Blast search analysis revealed that the C. dromedarius Hsp90α shared high similarity with other known Hsp90α. Comparative analyses of camel Hsp90α protein sequence with other mammalian Hsp90s showed high identity (85-94%). Heterologous expression of camel Hsp90α cDNA in E. coli JM109 (DE3) gave a fusion protein band of 86.0kDa after induction with IPTG for 4h.

KEYWORDS:

Arabian camel; Camelus dromedarius; Chaperones; Heat shock protein; Reverse transcription polymerase chain reaction

PMID:
26234578
DOI:
10.1016/j.ijbiomac.2015.07.058
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center