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Asian Journal of Biochemistry
  Year: 2015 | Volume: 10 | Issue: 1 | Page No.: 1-16
DOI: 10.3923/ajb.2015.1.16
 
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Identifying the Putative Interacting Partners of the Heat Shock Protein, HtpG through Phage Display Library Screening

Magdy M. Youssef and Mohammed A. Al-Omair

Abstract:
Heat Shock family of Proteins (HSPs) is conserved from prokaryotes to eukarutes and used as an antitumores. The mechanism of action of many antitumor proteins is still obscure in vivo. HtpG protein is a prokaryotic member of HSPs. In the present study, the htpG gene from E. coli was amplified by polymerase chain reaction and cloned in frame into the pGEX-2T DNA vector. The recombinant plasmid used to overexpress the GST-HtpG fusion protein. The GST-HtpG fusion and GST proteins were purified by chromatographic technique and applied with 15 mer phage library to identify polypeptidies which bind with the HtpG protein. Identification of such polypeptieds helped us to identify partner proteins that bind with the HSPs in vivo. Thirteen of the 15 mer amino acids sequences were also identified to bind with HtpG protein. Proteins that have homology sequences with the 15 mer amino acids sequences were identified from protein data base. The binding domain of the HSPs with client or partner proteins such as thyroid hormone receptor, protein kinase, nitric oxide synthase, SMC protein family, DNA polymerase, DNA topoisomerase, 50S ribosomal protein L2, ATP synthase, P53 and a quite number of proteins were detemined. This data indicate that the HtpG and HSPs bind with many proteins in vivo which could facilitate their protein folding.
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How to cite this article:

Magdy M. Youssef and Mohammed A. Al-Omair, 2015. Identifying the Putative Interacting Partners of the Heat Shock Protein, HtpG through Phage Display Library Screening. Asian Journal of Biochemistry, 10: 1-16.

DOI: 10.3923/ajb.2015.1.16

URL: https://scialert.net/abstract/?doi=ajb.2015.1.16

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