[No authors listed]
Nonsense-mediated decay (NMD) is a posttranscriptional surveillance mechanism in eukaryotes that recognizes and degrades transcripts with premature translation-termination codons. The RNA polymerase II C-terminal domain phosphatase-like protein FIERY2 (FRY2; also known as C-TERMINAL DOMAIN PHOSPHATASE-LIKE1 [CPL1]) plays multiple roles in RNA processing inArabidopsis thaliana Here, we found that FRY2/CPL1 interacts with twoNMDfactors, eIF4AIII and UPF3, and is involved in the dephosphorylation of eIF4AIII. This dephosphorylation retains eIF4AIII in the nucleus and limits its accumulation in the cytoplasm. By analyzing RNA-seq data combined with quantitative RT-PCR validation, we found that a subset of alternatively spliced transcripts and 5'-extended mRNAs withNMD-eliciting features accumulated in thefry2-1mutant, cycloheximide-treated wild type, andupf3mutant plants, indicating that FRY2 is essential for the degradation of theseNMDtranscripts.
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