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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Heterologous Expression of MeLEA3: A 10 kDa Late Embryogenesis Abundant Protein of Cassava, Confers Tolerance to Abiotic Stress in Escherichia coli with Recombinant Protein Showing In Vitro Chaperone Activity

Author(s): Nicolle L.F. Barros, Diehgo T. da Silva, Deyvid N. Marques, Fabiano M. de Brito, Savio P. dos Reis and Claudia R.B. de Souza

Volume 22 , Issue 8 , 2015

Page: [689 - 695] Pages: 7

DOI: 10.2174/0929866522666150520145302

Price: $65

Abstract

Late embryogenesis abundant (LEA) proteins are small molecular weight proteins involved in acquisition of tolerance to drought, salinity, high temperature, cold, and freezing stress in many plants. Previous studies revealed a cDNA sequence coding for a 10 kDa atypical LEA protein, named MeLEA3, predicted to be located into mitochondria with potential role in salt stress response of cassava (Manihot esculenta Crantz). Here we aimed to produce the recombinant MeLEA3 protein by heterologous expression in Escherichia coli and evaluate the tolerance of bacteria expressing this protein under abiotic stress. Our result revealed that the recombinant MeLEA3 protein conferred a protective function against heat and salt stress in bacterial cells. Also, the recombinant MeLEA3 protein showed in vitro chaperone activity by protection of NdeI restriction enzyme activity under heat stress.

Keywords: Abiotic stress, Atypical LEA protein, Cassava, Chaperone activity, Heterologous expression in bacteria, Recombinant protein.

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