The translation initiation factor, PeIF5B, from Pisum sativum displays chaperone activity |
| |
| Authors: | Suragani Madhuri Rasheedi Sheeba Hasnain Seyed E Ehtesham Nasreen Z |
| |
| Institution: | aMolecular Biology Unit, National Institute of Nutrition, Hyderabad 500 007, India;bLaboratory of Molecular and Cellular Biology, Centre for DNA Fingerprinting and Diagnostics, Hyderabad 500 001, India;cSchool of Biological Sciences, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110 016, India;dInstitute of Life Sciences, University of Hyderabad Campus, Hyderabad 500 046, India;eKing Saud University, Riyadh, Saudi Arabia;fInstitute of Liver and Biliary Sciences, D1, Vasant Kunj, New Delhi 110 070, India;gNational Institute of Pathology (NIP), Safdarjang Hospital Campus, New Delhi 110029, India |
| |
| Abstract: | We earlier documented the structural and functional characterization of PeIF5B factor from Pisum sativum that shows strong homology to the universal translation initiation factor eIF5B (Rasheedi et al., 2007, 2010 12] and 13]). We now show that PeIF5B is an unusually thermo-stable protein resisting temperatures up to 95 °C. PeIF5B prevents thermal aggregation of heat labile proteins, such as citrate synthase (CS) and NdeI, under heat stress or chemical denaturation conditions and promotes their functional folding. It also prevents the aggregation of DTT induced insulin reduction. GTP appears to stimulate PeIF5B-mediated chaperone activity. In-vivo, PeIF5B over expression significantly enhances, the viability of Escherichia coli cells after heat stress (50 °C). These observations lead us to conclude that PeIF5B, in addition to its role in protein translation, has chaperone like activity and could be likely involved in protein folding and protection from stress. |
| |
| Keywords: | Abbreviations: rPeIF5B recombinant PeIF5B CS citrate synthase GnHCl guanidine hydrochloride |
| 本文献已被 ScienceDirect PubMed 等数据库收录！ |
|
