Abstract
To analyze the mechanisms of salt-tolerance in a mangrove plant, Bruguiera sexangula, functional screening of the mangrove cDNAs encoding proteins essential for the salt-tolerance mechanisms was done using Eschericha coli. as the host organism. A transformant expression eukaryotic elongation factor 1A homologue (Bs-eEF1A) revealed to have enhanced salt and osmotic stress tolerance. In general, eEF1A is highly abundant protein responsible for the delivery of aminoacyl-tRNA to the accepter site of ribosomes during peptide chain elongation. It could not be explained why enhanced salt-tolerance was acquired in the E. coli transformant by expressing Bs-eEF1A. In this study, we show that Bs-eEF1A give rise to enhance heat shock stress tolerance in E. coli. Furthermore, we demonstrated that Bs-eEF1A has chaperone-like properties in vitro. These data suggest that Bs-eEF1A, in addition to its original function in translation elongation, might play an important role in the salt tolerance mechanisms of B. sexangula.
