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

被引:4
作者
Barros, Nicolle L. F. [1 ,2 ]
da Silva, Diehgo T. [1 ,3 ]
Marques, Deyvid N. [1 ,4 ]
de Brito, Fabiano M. [1 ,5 ]
dos Reis, Savio P. [1 ,4 ]
de Souza, Claudia R. B. [1 ]
机构
[1] Univ Fed Para UFPA, Inst Ciencias Biol, BR-66075110 Belem, Para, Brazil
[2] Bolsista Iniciacao Cient PIBIC UFPA CNPq, BR-66075110 Belem, Para, Brazil
[3] Programa Posgrad Neurociencias & Biol Celular UFP, BR-66075110 Belem, Para, Brazil
[4] Programa Posgrad Genet Biol Mol UFPA, BR-66075110 Belem, Para, Brazil
[5] Univ Fed Rural Amazonia, Programa Posgrad Agron, BR-66077530 Belem, Para, Brazil
关键词
Abiotic stress; Atypical LEA protein; Cassava; Chaperone activity; Heterologous expression in bacteria; Recombinant protein; HYDROPHOBIC LEA PROTEIN; MOLECULAR CHARACTERIZATION; SALT TOLERANCE; CITRUS; GENES; SEQUENCE; DROUGHT; DEHYDRIN; CDNA; IDENTIFICATION;
D O I
10.2174/0929866522666150520145302
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:689 / 695
页数:7
相关论文
共 50 条
[1]  
Amara I., 2014, American Journal of Plant Sciences, V5, P3440
[2]  
[Anonymous], PLANT PHYSL COMMUN
[3]   SEQUENCE AND CHARACTERIZATION OF 6 LEA PROTEINS AND THEIR GENES FROM COTTON [J].
BAKER, J ;
STEELE, C ;
DURE, L .
PLANT MOLECULAR BIOLOGY, 1988, 11 (03) :277-291
[4]   The enigmatic LEA proteins and other hydrophilins [J].
Battaglia, Marina ;
Olvera-Carrillo, Yadira ;
Garciarrubio, Alejandro ;
Campos, Francisco ;
Covarrubias, Alejandra A. .
PLANT PHYSIOLOGY, 2008, 148 (01) :6-24
[5]   Late Embryogenesis Abundant (LEA) proteins in legumes [J].
Battaglia, Marina ;
Covarrubias, Alejandra A. .
FRONTIERS IN PLANT SCIENCE, 2013, 4
[6]  
BIRNBOIM HC, 1979, NUCLEIC ACIDS RES, V7, P1513
[7]   MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins [J].
Boucher, Virginie ;
Buitink, Julia ;
Lin, Xiaodong ;
Boudet, Julie ;
Hoekstra, Folkert A. ;
Hundertmark, Michaela ;
Renard, Denis ;
Leprince, Olivier .
PLANT CELL AND ENVIRONMENT, 2010, 33 (03) :418-430
[8]   Dehydration-specific induction of hydrophilic protein genes in the anhydrobiotic nematode Aphelenchus avenae [J].
Browne, JA ;
Dolan, KM ;
Tyson, T ;
Goyal, K ;
Tunnacliffe, A ;
Burnell, AM .
EUKARYOTIC CELL, 2004, 3 (04) :966-975
[9]   Hydrophilic protein associated with desiccation tolerance exhibits broad protein stabilization function [J].
Chakrabortee, Sohini ;
Boschetti, Chiara ;
Walton, Laura J. ;
Sarkar, Sovan ;
Rubinsztein, David C. ;
Tunnacliffe, Alan .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (46) :18073-18078
[10]   Intrinsically disordered proteins as molecular shields [J].
Chakrabortee, Sohini ;
Tripathi, Rashmi ;
Watson, Matthew ;
Schierle, Gabriele S. Kaminski ;
Kurniawan, Davy P. ;
Kaminski, Clemens F. ;
Wise, Michael J. ;
Tunnacliffe, Alan .
MOLECULAR BIOSYSTEMS, 2012, 8 (01) :210-219