<Emphasis Type="Italic">Arabidopsis</Emphasis> immunophilins ROF1 (AtFKBP62) and ROF2 (AtFKBP65) exhibit tissue specificity,are heat-stress induced,and bind HSP90 |
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Authors: | Keren Aviezer-Hagai Julia Skovorodnikova Mario Galigniana Odelia Farchi-Pisanty Erez Maayan Shmuel Bocovza Yael Efrat Pascal von Koskull-Döring Nir Ohad Adina Breiman |
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Institution: | (1) Department of Plant Sciences, Tel Aviv University, Tel Aviv, Israel;(2) Instituto de Investigaciones Bioquimicas, Fundacion Instituto Leloir Buenos Aires, Buenos Aires, Argentina;(3) Institute of Molecular Bio Sciences, Goethe University, Frankfurt, Germany |
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Abstract: | The plant co-chaperones FK506-binding proteins (FKBPs) are peptidyl prolyl cis-trans isomerases that function in protein folding, signal transduction and chaperone activity. We report the characterization of
the Arabidopsis large FKBPs ROF1 (AtFKBP62) and ROF2 (AtFKBP65) expression and protein accumulation patterns. Transgenic plants expressing
ROF1 promoter fused to GUS reporter gene reveal that ROF1 expression is organ specific. High expression was observed in the
vascular elements of roots, in hydathodes and trichomes of leaves and in stigma, sepals, and anthers. The tissue specificity
and temporal expression of ROF1 and ROF2 show that they are developmentally regulated. Although ROF1 and ROF2 share 85% identity,
their expression in response to heat stress is differentially regulated. Both genes are induced in plants exposed to 37 °C,
but only ROF2 is a bonafide heat-stress protein, undetected when plants are grown at 22 °C. ROF1/ROF2 proteins accumulate
at 37 °C, remain stable for at least 4 h upon recovery at 22 °C, whereas, their mRNA level is reduced after 1 h at 22 °C.
By protein interaction assays, it was demonstrated, that ROF1 is a novel partner of HSP90. The five amino acids identified
as essential for recognition and interaction between the mammalian chaperones and HSP90 are conserved in the plant ROF1-HSP90.
We suggest that ROF/HSP90 complexes assemble in vivo. We propose that specific complexes formation between an HSP90 and ROF
isoforms depends on their spatial and temporal expression. Such complexes might be regulated by environmental conditions such
as heat stress or internal cues such as different hormones.
Electronic supplementary material Supplementary material is available in the online version of this article at and is accessible for authorized users. |
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Keywords: | ROF1/2 AtFKBP62/65 Immunophilins HSP90 TPR PPIase |
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