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Involvement of arabidopsis ROF2 (FKBP65) in thermotolerance
Year:
2010
Source of publication :
Plant Molecular Biology
Authors :
Cohen-Peer, Reut
;
.
Volume :
72
Co-Authors:
Meiri, D., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Tazat, K., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Cohen-Peer, R., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Farchi-Pisanty, O., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Aviezer-Hagai, K., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Avni, A., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Breiman, A., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Facilitators :
From page:
191
To page:
203
(
Total pages:
13
)
Abstract:
The ROF2 (FKBP65) is a heat stress protein which belongs to the FK506 Binding Protein (FKBP) family. It is homologous to ROF1 (FKBP62) which was recently shown to be involved in long term acquired thermotolerance by its interaction with HSP90.1 and modulation of the heat shock transcription factor HsfA2. In this study, we have demonstrated that ROF2 participates in long term acquired thermolerance, its mode of action being different from ROF1. In the absence of ROF2, the small heat shock proteins were highly expressed and the plants were resistant to heat stress, opposite to the effect observed in the absence of ROF1. It was further demonstrated that ROF2 transcription is modulated by HsfA2 which is also essential for keeping high levels of ROF2 during recovery from heat stress. ROF2 localization to the nucleus was observed several hours after heat stress exposure and its translocation to the nucleus was independent from the presence of HSP90.1 or HsfA2. ROF2 has been shown to interact with ROF1, to form heterodimers and it is suggested that via this interaction it can join the complex ROF1-HSP90.1- HsfA2. Transient expression of ROF2 together with ROF1 repressed transcription of small HSPs. A model describing the mode of action of ROF2 as a heat stress modulator which functions in negative feedback regulation of HsfA2 is proposed. © 2009 Springer Science+Business Media B.V.
Note:
Related Files :
arabidopsis
AtFKBP62
DNA binding protein
FK506
Genetics
Heat-Shock Proteins
Hsp90
metabolism
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Related Content
More details
DOI :
10.1007/s11103-009-9561-3
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
30329
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:53
Scientific Publication
Involvement of arabidopsis ROF2 (FKBP65) in thermotolerance
72
Meiri, D., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Tazat, K., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Cohen-Peer, R., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Farchi-Pisanty, O., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Aviezer-Hagai, K., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Avni, A., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Breiman, A., Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Involvement of arabidopsis ROF2 (FKBP65) in thermotolerance
The ROF2 (FKBP65) is a heat stress protein which belongs to the FK506 Binding Protein (FKBP) family. It is homologous to ROF1 (FKBP62) which was recently shown to be involved in long term acquired thermotolerance by its interaction with HSP90.1 and modulation of the heat shock transcription factor HsfA2. In this study, we have demonstrated that ROF2 participates in long term acquired thermolerance, its mode of action being different from ROF1. In the absence of ROF2, the small heat shock proteins were highly expressed and the plants were resistant to heat stress, opposite to the effect observed in the absence of ROF1. It was further demonstrated that ROF2 transcription is modulated by HsfA2 which is also essential for keeping high levels of ROF2 during recovery from heat stress. ROF2 localization to the nucleus was observed several hours after heat stress exposure and its translocation to the nucleus was independent from the presence of HSP90.1 or HsfA2. ROF2 has been shown to interact with ROF1, to form heterodimers and it is suggested that via this interaction it can join the complex ROF1-HSP90.1- HsfA2. Transient expression of ROF2 together with ROF1 repressed transcription of small HSPs. A model describing the mode of action of ROF2 as a heat stress modulator which functions in negative feedback regulation of HsfA2 is proposed. © 2009 Springer Science+Business Media B.V.
Scientific Publication
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