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A double-stranded RNA binding protein enhances drought resistance via protein phase separation in rice
A double-stranded RNA binding protein enhances drought resistance via protein phase separation in rice
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A double-stranded RNA binding protein enhances drought resistance via protein phase separation in rice
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A double-stranded RNA binding protein enhances drought resistance via protein phase separation in rice
A double-stranded RNA binding protein enhances drought resistance via protein phase separation in rice
Journal Article

A double-stranded RNA binding protein enhances drought resistance via protein phase separation in rice

2024
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Overview
Drought stress significantly impacts global rice production, highlighting the critical need to understand the genetic basis of drought resistance in rice. Here, through a genome-wide association study, we reveal that natural variations in DROUGHT RESISTANCE GENE 9 ( DRG9 ), encoding a double-stranded RNA (dsRNA) binding protein, contribute to drought resistance. Under drought stress, DRG9 condenses into stress granules (SGs) through liquid-liquid phase separation via a crucial α-helix. DRG9 recruits the mRNAs of OsNCED4 , a key gene for the biosynthesis of abscisic acid, into SGs and protects them from degradation. In drought-resistant DRG9 allele, natural variations in the coding region, causing an amino acid substitution (G267F) within the zinc finger domain, increase DRG9’s binding ability to OsNCED4 mRNA and enhance drought resistance. Introgression of the drought-resistant DRG9 allele into the elite rice Huanghuazhan significantly improves its drought resistance. Thus, our study underscores the role of a dsRNA-binding protein in drought resistance and its promising value in breeding drought-resistant rice. Drought is one of the major abiotic stresses affecting rice growth and development. Here, the authors identify a dsRNA-binding protein positively regulates rice drought resistance through promoting stability of OsNCED4 mRNAs, transcript of a key gene for the biosynthesis of abscisic acid, via protein phase separation.