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An abscisic-acid- and salt-stress-responsive rice cDNA from a novel plant gene family

Ann Moons (UGent) , Jan Gielen (UGent) , Joël Vandekerckhove (UGent) , Dominique Van Der Straeten (UGent) , Godelieve Gheysen (UGent) and Marc Van Montagu (UGent)
(1997) PLANTA. 202(4). p.443-454
Author
Organization
Abstract
A novel cDNA clone osr40c1, encoding a environment and belongs to a novel plant protein family that most probably has structural functions. abscisic acid (ABA)-responsive 40-kDa protein previously associated with salt tolerance (Moons et al. '1995' Plant Physiol 107: 177-186), was isolated from roots of rice seedlings (Oryza sativa L.). Exogenously applied ABA and salt shock induced a marked increase of the asr40c1 transcript level in roots of seedlings whereas constant osr40c1 mRNA levels were found in the shoot. The root-specific salinity-induced osr40c1 mRNA accumulation was rapid and gradually declined upon prolonged salt shock. Plant growth regulators, signalling the wounding and the pathogen response, did not enhance osr40c1 expression, indicating a salt- and osmotic-stress-specific response. The encoded OSR40c1 protein was found to be hydrophilic, rich in histidine residues (6%) constituting putative metal-binding domains, and to consist of a duplicated domain of 151 amino acids (75% identical), that can form amphiphilic a-helical structures. The gene osr40c1 belongs to a multigene family. Two osr40 genes were isolated, osr40g2 and osr40g3, tandemly arranged in an 8-kb region of the rice genome. Antisera raised against a conserved OSR40 peptide recognized different OSR40 proteins that accumulated in roots upon exposure to salt stress. The OSR40 protein family included 29-kDa proteins and two 40-kDa proteins, the latter most probably corresponding to OSR40c1 and OSR40g2 with duplicated domain structures. The osr40g3 transcript encoded a single copy of the OSR40 domain and exhibited a shoot-specific expression. Results indicate that OSR40c1 plays a role in the adaptative response of roots to an hyper-osmotic environment and belongs to a novel plant protein family that most probably has structural functions.
Keywords
EXPRESSION, MESSENGER-RNAS, HOMOLOGY, PROMOTER, BINDS, DNA, ELECTROPHORESIS, GLOBULAR-PROTEINS, salt stress, Oryza (salt stress), histidine-rich duplicated domain, gene expression (organ specific), abscisic acid, SECONDARY STRUCTURE, RECOGNITION SEQUENCE

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Chicago
Moons, Ann, Jan Gielen, Joël Vandekerckhove, Dominique Van Der Straeten, Godelieve Gheysen, and Marc Van Montagu. 1997. “An Abscisic-acid- and Salt-stress-responsive Rice cDNA from a Novel Plant Gene Family.” Planta 202 (4): 443–454.
APA
Moons, Ann, Gielen, J., Vandekerckhove, J., Van Der Straeten, D., Gheysen, G., & Van Montagu, M. (1997). An abscisic-acid- and salt-stress-responsive rice cDNA from a novel plant gene family. PLANTA, 202(4), 443–454.
Vancouver
1.
Moons A, Gielen J, Vandekerckhove J, Van Der Straeten D, Gheysen G, Van Montagu M. An abscisic-acid- and salt-stress-responsive rice cDNA from a novel plant gene family. PLANTA. 1997;202(4):443–54.
MLA
Moons, Ann, Jan Gielen, Joël Vandekerckhove, et al. “An Abscisic-acid- and Salt-stress-responsive Rice cDNA from a Novel Plant Gene Family.” PLANTA 202.4 (1997): 443–454. Print.
@article{184520,
  abstract     = {A novel cDNA clone osr40c1, encoding a environment and belongs to a novel plant protein family that most probably has structural functions. abscisic acid (ABA)-responsive 40-kDa protein previously associated with salt tolerance (Moons et al. '1995' Plant Physiol 107: 177-186), was isolated from roots of rice seedlings (Oryza sativa L.). Exogenously applied ABA and salt shock induced a marked increase of the asr40c1 transcript level in roots of seedlings whereas constant osr40c1 mRNA levels were found in the shoot. The root-specific salinity-induced osr40c1 mRNA accumulation was rapid and gradually declined upon prolonged salt shock. Plant growth regulators, signalling the wounding and the pathogen response, did not enhance osr40c1 expression, indicating a salt- and osmotic-stress-specific response. The encoded OSR40c1 protein was found to be hydrophilic, rich in histidine residues (6\%) constituting putative metal-binding domains, and to consist of a duplicated domain of 151 amino acids (75\% identical), that can form amphiphilic a-helical structures. The gene osr40c1 belongs to a multigene family. Two osr40 genes were isolated, osr40g2 and osr40g3, tandemly arranged in an 8-kb region of the rice genome. Antisera raised against a conserved OSR40 peptide recognized different OSR40 proteins that accumulated in roots upon exposure to salt stress. The OSR40 protein family included 29-kDa proteins and two 40-kDa proteins, the latter most probably corresponding to OSR40c1 and OSR40g2 with duplicated domain structures. The osr40g3 transcript encoded a single copy of the OSR40 domain and exhibited a shoot-specific expression. Results indicate that OSR40c1 plays a role in the adaptative response of roots to an hyper-osmotic environment and belongs to a novel plant protein family that most probably has structural functions.},
  author       = {Moons, Ann and Gielen, Jan and Vandekerckhove, Jo{\"e}l and Van Der Straeten, Dominique and Gheysen, Godelieve and Van Montagu, Marc},
  issn         = {0032-0935},
  journal      = {PLANTA},
  keyword      = {EXPRESSION,MESSENGER-RNAS,HOMOLOGY,PROMOTER,BINDS,DNA,ELECTROPHORESIS,GLOBULAR-PROTEINS,salt stress,Oryza (salt stress),histidine-rich duplicated domain,gene expression (organ specific),abscisic acid,SECONDARY STRUCTURE,RECOGNITION SEQUENCE},
  language     = {eng},
  number       = {4},
  pages        = {443--454},
  title        = {An abscisic-acid- and salt-stress-responsive rice cDNA from a novel plant gene family},
  url          = {http://dx.doi.org/10.1007/s004250050148},
  volume       = {202},
  year         = {1997},
}

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