A VQ-motif-containing protein fine-tunes rice immunity and growth by a hierarchical regulatory mechanism
Rice blast and bacterial blight, caused by the fungus Magnaporthe oryzae and the bacterium Xanthomonas oryzae pv. oryzae (Xoo), respectively, are devastating diseases affecting rice. Here, we report that a rice valine-glutamine (VQ) motif-containing protein, OsVQ25, balances broad-spectrum disease r...
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Published in | Cell reports (Cambridge) Vol. 40; no. 7; p. 111235 |
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Main Authors | , , , , , , , , , , , , , , , , , |
Format | Journal Article Web Resource |
Language | English |
Published |
Elsevier Inc
16.08.2022
Elsevier B.V |
Subjects | |
Online Access | Get full text |
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Summary: | Rice blast and bacterial blight, caused by the fungus Magnaporthe oryzae and the bacterium Xanthomonas oryzae pv. oryzae (Xoo), respectively, are devastating diseases affecting rice. Here, we report that a rice valine-glutamine (VQ) motif-containing protein, OsVQ25, balances broad-spectrum disease resistance and plant growth by interacting with a U-Box E3 ligase, OsPUB73, and a transcription factor, OsWRKY53. We show that OsPUB73 positively regulates rice resistance against M. oryzae and Xoo by interacting with and promoting OsVQ25 degradation via the 26S proteasome pathway. Knockout mutants of OsVQ25 exhibit enhanced resistance to both pathogens without a growth penalty. Furthermore, OsVQ25 interacts with and suppresses the transcriptional activity of OsWRKY53, a positive regulator of plant immunity. OsWRKY53 downstream defense-related genes and brassinosteroid signaling genes are upregulated in osvq25 mutants. Our findings reveal a ubiquitin E3 ligase-VQ protein-transcription factor module that fine-tunes plant immunity and growth at the transcriptional and posttranslational levels.
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•The U-box E3 ligase OsPUB73 positively regulates broad-spectrum disease resistance•OsPUB73 interacts with and promotes the degradation of the VQ-motif protein OsVQ25•The osvq25 mutant confers broad-spectrum disease resistance without a growth penalty•OsVQ25 interacts with and suppresses the transcriptional activity of OsWRKY53
Hao et al. show that loss-function of a VQ-motif-containing protein OsVQ25 confers broad-spectrum disease resistance. A U-box E3 ligase OsPUB73 interacts with and degrades OsVQ25, while OsVQ25 suppresses the transcriptional activity of a transcription factor OsWRKY53, highlighting that OsVQ25 balances plant immunity and growth by a hierarchical regulatory mechanism. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 scopus-id:2-s2.0-85135961635 |
ISSN: | 2211-1247 2211-1247 |
DOI: | 10.1016/j.celrep.2022.111235 |