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dc.contributor.author
Aviezer-Hagai, Keren
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Skovorodnikova, Julia
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Galigniana, Mario Daniel
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Farchi Pisanty, Odelia
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Maayan, Erez
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Bocovza, Shmuel
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Efrat, Yael
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Von Koskull Döring, Pascal
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Ohad, Nir
dc.contributor.author
Breiman, Adina
dc.date.available
2021-06-11T13:00:53Z
dc.date.issued
2007-01
dc.identifier.citation
Aviezer-Hagai, Keren; Skovorodnikova, Julia; Galigniana, Mario Daniel; Farchi Pisanty, Odelia; Maayan, Erez; et al.; Arabidopsis immunophilins ROF1 (AtFKBP62) and ROF2 (AtFKBP65) exhibit tissue specificity, are heat-stress induced, and bind HSP90; Springer; Plant Molecular Biology; 63; 2; 1-2007; 237-255
dc.identifier.issn
0167-4412
dc.identifier.uri
http://hdl.handle.net/11336/133668
dc.description.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 degrees C, but only ROF2 is a bonafide heat-stress protein, undetected when plants are grown at 22 degrees C. ROF1/ROF2 proteins accumulate at 37 degrees C, remain stable for at least 4 h upon recovery at 22 degrees C, whereas, their mRNA level is reduced after 1 h at 22 degrees 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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
ATFKBP62/65
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HSP90
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IMMUNOPHILINS
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PPIASE
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ROF1/2
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TPR
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Endocrinología y Metabolismo
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Medicina Clínica
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CIENCIAS MÉDICAS Y DE LA SALUD
dc.title
Arabidopsis immunophilins ROF1 (AtFKBP62) and ROF2 (AtFKBP65) exhibit tissue specificity, are heat-stress induced, and bind HSP90
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2021-06-07T16:56:08Z
dc.journal.volume
63
dc.journal.number
2
dc.journal.pagination
237-255
dc.journal.pais
Alemania
dc.description.fil
Fil: Aviezer-Hagai, Keren. Universitat Tel Aviv; Israel
dc.description.fil
Fil: Skovorodnikova, Julia. Universitat Tel Aviv; Israel
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Fil: Galigniana, Mario Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
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Fil: Farchi Pisanty, Odelia. Universitat Tel Aviv; Israel
dc.description.fil
Fil: Maayan, Erez. Universitat Tel Aviv; Israel
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Fil: Bocovza, Shmuel. Universitat Tel Aviv; Israel
dc.description.fil
Fil: Efrat, Yael. Universitat Tel Aviv; Israel
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Fil: Von Koskull Döring, Pascal. Goethe Universitat Frankfurt; Alemania
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Fil: Ohad, Nir. Universitat Tel Aviv; Israel
dc.description.fil
Fil: Breiman, Adina. Universitat Tel Aviv; Israel
dc.journal.title
Plant Molecular Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs11103-006-9085-z
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info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/ 10.1007/s11103-006-9085-z