Plant Hsp100/ClpB-like proteins: poorly-analyzed cousins of yeast ClpB machine.
ClpB/Hsp100 proteins act as chaperones, mediating disaggregation of denatured proteins. Recent work shows that apart from cytoplasm, these proteins are localized to nuclei, chloroplasts, mitochondria and plasma membrane. While ClpB/Hsp100 genes are essentially stress-induced (mainly heat stress) in vegetative organs of the plant body, expression of ClpB/Hsp100 proteins is noted to be constitutive in plant reproductive structures like pollen grains, developing embryos, seeds etc. With global warming looming large on the horizon, ways to genetically engineer plants against high temperature stress are urgently needed. Yeast mutants unable to synthesize active ClpB/Hsp100 protein show a clear thermosensitive phenotype. ClpB/Hsp100 proteins are implicated in high temperature stress tolerance in plants. We herein highlight the selected important facets of this protein family in plants.
Singh
Amanjot
A
Department of Plant Molecular Biology, University of Delhi South Campus, New Delhi, 110021, India.
Grover
Anil
A
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000235:genetics / Q000502:physiology*; D018869:Heat-Shock Response; D008969:Molecular Sequence Data; D012275:Oryza / Q000235:genetics / Q000378:metabolism; D010802:Phylogeny; D010940:Plant Proteins / Q000235:genetics / Q000502:physiology*; D016415:Sequence Alignment; D015003:Yeasts / Q000235:genetics / Q000378:metabolism
D006360:Heat-Shock Proteins; D010940:Plant Proteins
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