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Sumoylation of Arabidopsis heat shock factor A2 (HsfA2) modifies its activity during acquired thermotholerance
Year:
2010
Source of publication :
Plant Molecular Biology
Authors :
Cohen-Peer, Reut
;
.
Volume :
74
Co-Authors:
Cohen-Peer, R., Department of Plant Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Schuster, S., Department of Plant Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Meiri, D., Department of Plant Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Breiman, A., Department of Plant Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Avni, A., Department of Plant Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Facilitators :
From page:
33
To page:
45
(
Total pages:
13
)
Abstract:
Post-translational modification of target proteins by the small ubiquitin-like modifier protein (SUMO) regulate many cellular processes. In this work we show SUMOylation of the heat shock transcription factor, AtHsfA2, in connection with the plant's response to heat stress and acquired thermotolerance. Using the Yeast two hybrid and the bimolecular fluorescence complementation system, we have found that AtSUMO1 physically interacts with AtHsfA2. Further investigation allowed us to determine that Lys 315 of AtHsfA2 is the main SUMOylation site. Overexpression of AtSUMO1 led to a decrease in AtHsfA2 transcriptional activation of heat shock promoters. We have examined the effect of AtSUMO1 on AtHsfA2 during heat shock treatments. The phenotype of seedlings overexpressing AtSUMO1 resembled the phenotype of AtHsfA2 knock out seedlings, which were more sensitive than wild type seedlings to repeated heat treatment. Furthermore, AtSUMO1 overexpressing seedlings exhibited lower expression levels of small heat shock proteins as compared with wild type seedlings after heat treatment. Based on our findings, we suggest that AtSUMO1 is involved in the regulation of AtHsfA2 in acquired thermotolerance. © 2010 Springer Science+Business Media B.V.
Note:
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More details
DOI :
10.1007/s11103-010-9652-1
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
27179
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:28
Scientific Publication
Sumoylation of Arabidopsis heat shock factor A2 (HsfA2) modifies its activity during acquired thermotholerance
74
Cohen-Peer, R., Department of Plant Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Schuster, S., Department of Plant Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Meiri, D., Department of Plant Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Breiman, A., Department of Plant Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Avni, A., Department of Plant Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Sumoylation of Arabidopsis heat shock factor A2 (HsfA2) modifies its activity during acquired thermotholerance
Post-translational modification of target proteins by the small ubiquitin-like modifier protein (SUMO) regulate many cellular processes. In this work we show SUMOylation of the heat shock transcription factor, AtHsfA2, in connection with the plant's response to heat stress and acquired thermotolerance. Using the Yeast two hybrid and the bimolecular fluorescence complementation system, we have found that AtSUMO1 physically interacts with AtHsfA2. Further investigation allowed us to determine that Lys 315 of AtHsfA2 is the main SUMOylation site. Overexpression of AtSUMO1 led to a decrease in AtHsfA2 transcriptional activation of heat shock promoters. We have examined the effect of AtSUMO1 on AtHsfA2 during heat shock treatments. The phenotype of seedlings overexpressing AtSUMO1 resembled the phenotype of AtHsfA2 knock out seedlings, which were more sensitive than wild type seedlings to repeated heat treatment. Furthermore, AtSUMO1 overexpressing seedlings exhibited lower expression levels of small heat shock proteins as compared with wild type seedlings after heat treatment. Based on our findings, we suggest that AtSUMO1 is involved in the regulation of AtHsfA2 in acquired thermotolerance. © 2010 Springer Science+Business Media B.V.
Scientific Publication
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