MYB30 transcription factor regulates oxidative and heat stress responses through ANNEXIN-mediated cytosolic calcium signaling in Arabidopsis
Cytosolic calcium signaling is critical for regulating downstream responses in plants encountering unfavorable environmental conditions. In a genetic screen for Arabidopsis thaliana mutants defective in stress-induced cytosolic free Ca2+ ([Ca2+]cyt) elevations, we identified the R2R3-MYB transcripti...
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Published in | The New phytologist Vol. 216; no. 1; pp. 163 - 177 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
England
New Phytologist Trust
01.10.2017
Wiley Subscription Services, Inc |
Subjects | |
Online Access | Get full text |
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Summary: | Cytosolic calcium signaling is critical for regulating downstream responses in plants encountering unfavorable environmental conditions.
In a genetic screen for Arabidopsis thaliana mutants defective in stress-induced cytosolic free Ca2+ ([Ca2+]cyt) elevations, we identified the R2R3-MYB transcription factor MYB30 as a regulator of [Ca2+]cyt in response to H2O2 and heat stresses.
Plants lacking MYB30 protein exhibited greater elevation of [Ca2+]cyt in response to oxidative and heat stimuli. Real-time reverse transcription–polymerase chain reaction (RT-PCR) results indicated that the expression of a number of ANNEXIN (ANN) genes, which encode Ca2+-regulated membrane-binding proteins modulating cytosolic calcium signatures, were upregulated in myb30 mutants. Further analysis showed that MYB30 bound to the promoters of ANN1 and ANN4 and repressed their expression. myb30 mutants were sensitive to methyl viologen (MV) and heat stresses. The H2O2- and heat-induced abnormal [Ca2+]cyt in myb30 was dependent on the function of ANN proteins. Moreover, the MV and heat sensitivity of myb30 was suppressed in mutants lacking ANN function or by application of LaCl3, a calcium channel blocker.
These results indicate that MYB30 regulates oxidative and heat stress responses through calcium signaling, which is at least partially mediated by ANN1 and ANN4. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
ISSN: | 0028-646X 1469-8137 1469-8137 |
DOI: | 10.1111/nph.14679 |