Abstract
Rice seedlings accumulate stainable amounts of the 104 and 90 kDa polypeptides in response to high temperature stress. We have purified and raised highly specific polyclonal antisera against both of these polypeptides. In western blotting experiments, we find that these proteins are accumulated to different extents in rice seedlings subjected to salinity (NaCl), water stress, low-temperature stress and exogenous abscisic acid application. These proteins also accumulated when rice seedlings grown in pots under natural conditions were subjected to water stress by withholding watering. Seedlings of Triticum aestivum, Sorghum bicolor, Pisum sativum, Zea mays, Brassica juncea and mycelium of Neurospora crassa showed accumulation of the immunological homologues of both the 104 and the 90 kDa polypeptides, in response to high-temperature stress. We have earlier shown that shoots of rice seedlings exposed to heat shock accumulate a 110 kDa polypeptide which is an immunological homologue of the yeast HSP 104 (Singla and Grover, Plant Mol Biol 22: 1177-1180, 1993). Employing anti-rice HSP 104 antibodies and anti-yeast HSP 104 antibodies together, we provide evidence that rice HSP 104 is different from the earlier characterized rice HSP 110.
MeSH Terms
Adaptation, Biological
Blotting, Western
HSP90 Heat-Shock Proteins/immunology,isolation & purification
Heat-Shock Proteins/immunology,isolation & purification
Heat-Shock Response
Oryza/physiology
Plant Physiological Phenomena
Plant Proteins/immunology,isolation & purification
Species Specificity
Tissue Distribution
Chemicals
HSP90 Heat-Shock Proteins
Heat-Shock Proteins
Plant Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Pareek A
Department of Plant Molecular Biology, University of Delhi South Campus, India.
Singla S L
Grover A
References (18)
18 references, click to expand
-
hsp80 of Neurospora crassa: cDNA cloning, gene mapping, and studies of mRNA accumulation under stress.
Biochem Cell Biol. 1992 Dec;70(12):1356-67
PMID: 1363716
-
HSP104 required for induced thermotolerance.
Science. 1990 Jun 1;248(4959):1112-5
PMID: 2188365
-
Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
Nature. 1970 Aug 15;227(5259):680-5
PMID: 5432063
-
Hsp104 is required for tolerance to many forms of stress.
EMBO J. 1992 Jun;11(6):2357-64
PMID: 1600951
-
Heat-inducible rice hsp82 and hsp70 are not always co-regulated.
Planta. 1994;193(1):57-66
PMID: 7764623
-
Protein disaggregation mediated by heat-shock protein Hsp104.
Nature. 1994 Dec 1;372(6505):475-8
PMID: 7984243
-
The heat-shock proteins.
Annu Rev Genet. 1988;22:631-77
PMID: 2853609
-
HSP90 homologue from Madagascar periwinkle (Catharanthus roseus): cDNA sequence, regulation of protein expression and location in the endoplasmic reticulum.
Plant Mol Biol. 1993 Nov;23(3):583-94
PMID: 8106014
-
A pathogen-induced gene of barley encodes a HSP90 homologue showing striking similarity to vertebrate forms resident in the endoplasmic reticulum.
Plant Mol Biol. 1993 Mar;21(6):1097-108
PMID: 8490130
-
Solubilization of plant membrane proteins for analysis by two-dimensional gel electrophoresis.
Plant Physiol. 1986 Jul;81(3):802-6
PMID: 16664906
-
Expression of Low Molecular Weight Heat-Shock Proteins under Field Conditions.
Plant Physiol. 1993 Apr;101(4):1209-1216
PMID: 12231775
-
The heat-shock response.
Annu Rev Biochem. 1986;55:1151-91
PMID: 2427013
-
Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae.
Mol Gen Genet. 1994 Mar;242(5):517-27
PMID: 8121410
-
Protein folding in the cell.
Nature. 1992 Jan 2;355(6355):33-45
PMID: 1731198
-
An Arabidopsis heat shock protein complements a thermotolerance defect in yeast.
Plant Cell. 1994 Dec;6(12):1899-909
PMID: 7866032
-
A soybean 101-kD heat shock protein complements a yeast HSP104 deletion mutant in acquiring thermotolerance.
Plant Cell. 1994 Dec;6(12):1889-97
PMID: 7866031
-
Antibodies raised against yeast HSP 104 cross-react with a heat- and abscisic acid-regulated polypeptide in rice.
Plant Mol Biol. 1993 Sep;22(6):1177-80
PMID: 8400134
-
Hsp104 is a highly conserved protein with two essential nucleotide-binding sites.
Nature. 1991 Sep 19;353(6341):270-3
PMID: 1896074