Non-redundant functions of sHSP-CIs in acquired thermotolerance and their role in early seed development in Arabidopsis

Mery Dafny-Yelin, Tzvi Tzfira, Alexander Vainstein, Zach Adam

Research output: Contribution to journalArticlepeer-review

58 Scopus citations


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.

Original languageEnglish
Pages (from-to)363-373
Number of pages11
JournalPlant Molecular Biology
Issue number4
StatePublished - 1 Jul 2008
Externally publishedYes


  • Hypocotyl elongation
  • Petals
  • Rose
  • Seed development
  • sHSP-CI

ASJC Scopus subject areas

  • Agronomy and Crop Science
  • Genetics
  • Plant Science


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