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The conjugation of SUMO to the transcription factor MYC2 functions in blue light-mediated seedling development in Arabidopsis
A key function of photoreceptor signaling is the coordinated regulation of a large number of genes to optimize plant growth and development. The basic helix loop helix (bHLH) transcription factor MYC2 is crucial for regulating gene expression in Arabidopsis thaliana during development in blue light....
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9338799/ https://www.ncbi.nlm.nih.gov/pubmed/35567527 http://dx.doi.org/10.1093/plcell/koac142 |
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author | Srivastava, Moumita Srivastava, Anjil Kumar Roy, Dipan Mansi, Mansi Gough, Catherine Bhagat, Prakash Kumar Zhang, Cunjin Sadanandom, Ari |
author_facet | Srivastava, Moumita Srivastava, Anjil Kumar Roy, Dipan Mansi, Mansi Gough, Catherine Bhagat, Prakash Kumar Zhang, Cunjin Sadanandom, Ari |
author_sort | Srivastava, Moumita |
collection | PubMed |
description | A key function of photoreceptor signaling is the coordinated regulation of a large number of genes to optimize plant growth and development. The basic helix loop helix (bHLH) transcription factor MYC2 is crucial for regulating gene expression in Arabidopsis thaliana during development in blue light. Here we demonstrate that blue light induces the SUMOylation of MYC2. Non-SUMOylatable MYC2 is less effective in suppressing blue light-mediated photomorphogenesis than wild-type (WT) MYC2. MYC2 interacts physically with the SUMO proteases SUMO PROTEASE RELATED TO FERTILITY1 (SPF1) and SPF2. Blue light exposure promotes the degradation of SPF1 and SPF2 and enhances the SUMOylation of MYC2. Phenotypic analysis revealed that SPF1/SPF2 function redundantly as positive regulators of blue light-mediated photomorphogenesis. Our data demonstrate that SUMO conjugation does not affect the dimerization of MYC transcription factors but modulates the interaction of MYC2 with its cognate DNA cis-element and with the ubiquitin ligase Plant U-box 10 (PUB10). Finally, we show that non-SUMOylatable MYC2 is less stable and interacts more strongly with PUB10 than the WT. Taken together, we conclude that SUMO functions as a counterpoint to the ubiquitin-mediated degradation of MYC2, thereby enhancing its function in blue light signaling. |
format | Online Article Text |
id | pubmed-9338799 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-93387992022-08-01 The conjugation of SUMO to the transcription factor MYC2 functions in blue light-mediated seedling development in Arabidopsis Srivastava, Moumita Srivastava, Anjil Kumar Roy, Dipan Mansi, Mansi Gough, Catherine Bhagat, Prakash Kumar Zhang, Cunjin Sadanandom, Ari Plant Cell Research Articles A key function of photoreceptor signaling is the coordinated regulation of a large number of genes to optimize plant growth and development. The basic helix loop helix (bHLH) transcription factor MYC2 is crucial for regulating gene expression in Arabidopsis thaliana during development in blue light. Here we demonstrate that blue light induces the SUMOylation of MYC2. Non-SUMOylatable MYC2 is less effective in suppressing blue light-mediated photomorphogenesis than wild-type (WT) MYC2. MYC2 interacts physically with the SUMO proteases SUMO PROTEASE RELATED TO FERTILITY1 (SPF1) and SPF2. Blue light exposure promotes the degradation of SPF1 and SPF2 and enhances the SUMOylation of MYC2. Phenotypic analysis revealed that SPF1/SPF2 function redundantly as positive regulators of blue light-mediated photomorphogenesis. Our data demonstrate that SUMO conjugation does not affect the dimerization of MYC transcription factors but modulates the interaction of MYC2 with its cognate DNA cis-element and with the ubiquitin ligase Plant U-box 10 (PUB10). Finally, we show that non-SUMOylatable MYC2 is less stable and interacts more strongly with PUB10 than the WT. Taken together, we conclude that SUMO functions as a counterpoint to the ubiquitin-mediated degradation of MYC2, thereby enhancing its function in blue light signaling. Oxford University Press 2022-05-14 /pmc/articles/PMC9338799/ /pubmed/35567527 http://dx.doi.org/10.1093/plcell/koac142 Text en � The Author(s) 2022. Published by Oxford University Press on behalf of American Society of Plant Biologists. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Srivastava, Moumita Srivastava, Anjil Kumar Roy, Dipan Mansi, Mansi Gough, Catherine Bhagat, Prakash Kumar Zhang, Cunjin Sadanandom, Ari The conjugation of SUMO to the transcription factor MYC2 functions in blue light-mediated seedling development in Arabidopsis |
title | The conjugation of SUMO to the transcription factor MYC2 functions in blue light-mediated seedling development in Arabidopsis |
title_full | The conjugation of SUMO to the transcription factor MYC2 functions in blue light-mediated seedling development in Arabidopsis |
title_fullStr | The conjugation of SUMO to the transcription factor MYC2 functions in blue light-mediated seedling development in Arabidopsis |
title_full_unstemmed | The conjugation of SUMO to the transcription factor MYC2 functions in blue light-mediated seedling development in Arabidopsis |
title_short | The conjugation of SUMO to the transcription factor MYC2 functions in blue light-mediated seedling development in Arabidopsis |
title_sort | conjugation of sumo to the transcription factor myc2 functions in blue light-mediated seedling development in arabidopsis |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9338799/ https://www.ncbi.nlm.nih.gov/pubmed/35567527 http://dx.doi.org/10.1093/plcell/koac142 |
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