TY - JOUR
T1 - The RNA Polymerase II C-Terminal Domain Phosphatase-Like Protein FIERY2/CPL1 Interacts with eIF4AIII and Is Essential for Nonsense-Mediated mRNA Decay in Arabidopsis
AU - Cui, Peng
AU - Chen, Tao
AU - Qin, Tao
AU - Ding, Feng
AU - Wang, Zhenyu
AU - Chen, Hao
AU - Xiong, Liming
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): BAS/1/1007-1-1, URF/1/2283-01-01
Acknowledgements: This work was supported by King Abdullah University of Science and Technology Office of Sponsored Research (OSR) under Award URF/1/2283-01-01 and Faculty Baseline Funds BAS/1/1007-1-1. We thank the Bioscience Core Lab of KAUST for providing genome sequencing and imaging services.
PY - 2016/2/17
Y1 - 2016/2/17
N2 - © 2016 American Society of Plant Biologists. All rights reserved. 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 in Arabidopsis thaliana. Here, we found that FRY2/CPL1 interacts with two NMD factors, 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 59-extended mRNAs with NMD-eliciting features accumulated in the fry2-1 mutant, cycloheximidetreated wild type, and upf3 mutant plants, indicating that FRY2 is essential for the degradation of these NMD transcripts.
AB - © 2016 American Society of Plant Biologists. All rights reserved. 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 in Arabidopsis thaliana. Here, we found that FRY2/CPL1 interacts with two NMD factors, 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 59-extended mRNAs with NMD-eliciting features accumulated in the fry2-1 mutant, cycloheximidetreated wild type, and upf3 mutant plants, indicating that FRY2 is essential for the degradation of these NMD transcripts.
UR - http://hdl.handle.net/10754/621443
UR - http://www.plantcell.org/lookup/doi/10.1105/tpc.15.00771
UR - http://www.scopus.com/inward/record.url?scp=84962850768&partnerID=8YFLogxK
U2 - 10.1105/tpc.15.00771
DO - 10.1105/tpc.15.00771
M3 - Article
C2 - 26887918
SN - 1040-4651
VL - 28
SP - 770
EP - 785
JO - The Plant Cell
JF - The Plant Cell
IS - 3
ER -