TY - JOUR
T1 - Non-redundant functions of sHSP-CIs in acquired thermotolerance and their role in early seed development in Arabidopsis
AU - Dafny-Yelin, Mery
AU - Tzfira, Tzvi
AU - Vainstein, Alexander
AU - Adam, Zach
N1 - Funding Information:
Acknowledgements This work was supported in part by the Israel Science Foundation (grant no. 466/01). We wish to thank Ifaat Laskar for technical assistance, Prof. David Weiss and Dr. Adi Zaltsman for helpful advice in the course of this study, and Ronit Rimon and Noa Wigoda for critical reading of the manuscript.
PY - 2008/7/1
Y1 - 2008/7/1
N2 - Heat-shock proteins (HSPs) are a group of evolutionarily conserved polypeptides whose expression is induced in all organisms in response to environmental stresses and during various developmental processes. In this work, we show that the rose (Rosa hybrida) cytoplasmic 17.5-kDa Class I small HSP (sHSP17.5-CI, accession number: BQ103946) increases dramatically during flower development, and accumulates in closed bud petals and leaves only in response to heat stress. mRNA for a putative ortholog of this protein is also found in petals, but not leaves, of Arabidopsis (Arabidopsis thaliana) plants grown under optimal conditions, and it accumulates in leaves in response to heat stress. Analysis of Arabidopsis T-DNA insertion lines affected at three homologous genes revealed that their acquired thermotolerance, as measured by hypocotyl-elongation assay, is impaired. The correlation between sHSP-CI accumulation and expansion of rose petal cells, impairment of acquired thermotolerance, and defects in early embryogenesis of the double mutants (hsp17.4/hsp17.6A), all suggest that sHSP-CI proteins play a role in protecting cell proteins at various developmental stages, whereas in hypocotyl elongation they have a non-redundant function in acquired thermotolerance but have a redundant function in early embryogenesis.
AB - Heat-shock proteins (HSPs) are a group of evolutionarily conserved polypeptides whose expression is induced in all organisms in response to environmental stresses and during various developmental processes. In this work, we show that the rose (Rosa hybrida) cytoplasmic 17.5-kDa Class I small HSP (sHSP17.5-CI, accession number: BQ103946) increases dramatically during flower development, and accumulates in closed bud petals and leaves only in response to heat stress. mRNA for a putative ortholog of this protein is also found in petals, but not leaves, of Arabidopsis (Arabidopsis thaliana) plants grown under optimal conditions, and it accumulates in leaves in response to heat stress. Analysis of Arabidopsis T-DNA insertion lines affected at three homologous genes revealed that their acquired thermotolerance, as measured by hypocotyl-elongation assay, is impaired. The correlation between sHSP-CI accumulation and expansion of rose petal cells, impairment of acquired thermotolerance, and defects in early embryogenesis of the double mutants (hsp17.4/hsp17.6A), all suggest that sHSP-CI proteins play a role in protecting cell proteins at various developmental stages, whereas in hypocotyl elongation they have a non-redundant function in acquired thermotolerance but have a redundant function in early embryogenesis.
KW - Hypocotyl elongation
KW - Petals
KW - Rose
KW - Seed development
KW - sHSP-CI
UR - http://www.scopus.com/inward/record.url?scp=44649168147&partnerID=8YFLogxK
U2 - 10.1007/s11103-008-9326-4
DO - 10.1007/s11103-008-9326-4
M3 - Article
AN - SCOPUS:44649168147
SN - 0167-4412
VL - 67
SP - 363
EP - 373
JO - Plant Molecular Biology
JF - Plant Molecular Biology
IS - 4
ER -