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

Handle URI:
http://hdl.handle.net/10754/621443
Title:
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
Authors:
Cui, Peng ( 0000-0003-3076-0070 ) ; Chen, Tao; Qin, Tao; Ding, Feng ( 0000-0001-8237-4062 ) ; Wang, Zhenyu; Chen, Hao; Xiong, Liming ( 0000-0001-8099-0806 )
Abstract:
© 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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Cui P, Chen T, Qin T, Ding F, Wang Z, et al. (2016) 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. Plant Cell 28: 770–785. Available: http://dx.doi.org/10.1105/tpc.15.00771.
Publisher:
American Society of Plant Biologists (ASPB)
Journal:
The Plant Cell
Issue Date:
18-Feb-2016
DOI:
10.1105/tpc.15.00771
Type:
Article
ISSN:
1040-4651; 1532-298X
Sponsors:
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.
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorCui, Pengen
dc.contributor.authorChen, Taoen
dc.contributor.authorQin, Taoen
dc.contributor.authorDing, Fengen
dc.contributor.authorWang, Zhenyuen
dc.contributor.authorChen, Haoen
dc.contributor.authorXiong, Limingen
dc.date.accessioned2016-11-03T08:29:26Z-
dc.date.available2016-11-03T08:29:26Z-
dc.date.issued2016-02-18en
dc.identifier.citationCui P, Chen T, Qin T, Ding F, Wang Z, et al. (2016) 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. Plant Cell 28: 770–785. Available: http://dx.doi.org/10.1105/tpc.15.00771.en
dc.identifier.issn1040-4651en
dc.identifier.issn1532-298Xen
dc.identifier.doi10.1105/tpc.15.00771en
dc.identifier.urihttp://hdl.handle.net/10754/621443-
dc.description.abstract© 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.en
dc.description.sponsorshipThis 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.en
dc.publisherAmerican Society of Plant Biologists (ASPB)en
dc.titleThe RNA Polymerase II C-Terminal Domain Phosphatase-Like Protein FIERY2/CPL1 Interacts with eIF4AIII and Is Essential for Nonsense-Mediated mRNA Decay in Arabidopsisen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalThe Plant Cellen
dc.contributor.institutionBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, Chinaen
dc.contributor.institutionMonsanto Co., St. Louis, MO, United Statesen
kaust.authorCui, Pengen
kaust.authorChen, Taoen
kaust.authorQin, Taoen
kaust.authorDing, Fengen
kaust.authorWang, Zhenyuen
kaust.authorChen, Haoen
kaust.authorXiong, Limingen
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