[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

Suragani, M. and Rasheedi, S. and Hasnain, S.E. and Ehtesham, N.Z. (2011) The translation initiation factor, PeIF5B, from Pisum sativum displays chaperone activity. Biochemical and Biophysical Research Communications, 414 (2). pp. 390-396. ISSN 0006-291X

[img] Text
BBRC 414 p390.pdf
Restricted to Repository staff only

Download (474Kb) | Request a copy

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 [12,13]). We now show that PeIF5B is an unusually thermo-stable protein resisting temperatures up to 95C. 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 (50C). 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. © 2011 Elsevier Inc.

Item Type: Article
Depositing User: Dr P Divakar
Date Deposited: 31 Oct 2015 20:58
Last Modified: 31 Oct 2015 20:58
URI: http://cdfd.sciencecentral.in/id/eprint/592

Actions (login required)

View Item View Item