ArticleProceedings of the National Academy of Sciences of the United States of America2004
Arabidopsis C-terminal domain phosphatase-like 1 and 2 are essential Ser-5-specific C-terminal domain phosphatases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 127 citations in OpenAlex.
- Heat stress triggers enhanced nuclear localization of HYPONASTIC LEAVES 1 to regulate microRNA biogenesis and thermotolerance in plants.The Plant cell · 2025Article
- C-TERMINAL DOMAIN PHOSPHATASE-LIKE 1 promotes flowering with TAF15b by repressing the floral repressor gene FLOWERING LOCUS C.Molecules and cells · 2024Article
- Identification and Functional Analysis ofInternational journal of molecular sciences · 2024Article
- A dephosphorylation-dependent molecular switch for FT repression mediates flowering in Arabidopsis.Plant communications · 2024Article
- Identification and characterization of RNA polymerase II (RNAP) C-Terminal domain phosphatase-like 3 (SlCPL3) in tomato under biotic stress.Molecular biology reports · 2023Article
- Hyponastic Leaves 1 Interacts with RNA Pol II to Ensure Proper Transcription of MicroRNA Genes.Plant & cell physiology · 2023Article
- A gene silencing screen uncovers diverse tools for targeted gene repression in Arabidopsis.Nature plants · 2023Article
- The plant FYVE domain-containing protein FREE1 associates with microprocessor components to repress miRNA biogenesis.EMBO reports · 2023Article
- CPL2 and CPL3 act redundantly inPlant signaling & behavior · 2022Article
- The intersection between circadian and heat-responsive regulatory networks controls plant responses to increasing temperatures.Biochemical Society transactions · 2022Review
- A Molecular switch for FLOWERING LOCUS C activation determines flowering time in Arabidopsis.The Plant cell · 2022Article
- Review
- C-terminal domain phosphatase-like 1 (CPL1) is involved in floral transition in Arabidopsis.BMC genomics · 2021Article
- Article
- Coupling of H3K27me3 recognition with transcriptional repression through the BAH-PHD-CPL2 complex in Arabidopsis.Nature communications · 2020Article
- Emerging Roles of RNA-Binding Proteins in Seed Development and Performance.International journal of molecular sciences · 2020Review
- ECERIFERUM11/C-TERMINAL DOMAIN PHOSPHATASE-LIKE2 Affects Secretory Trafficking.Plant physiology · 2019Article
- Alternative Splicing and Transcription Elongation in Plants.Frontiers in plant science · 2019Review
- The Arabidopsis RNA Polymerase II Carboxyl Terminal Domain (CTD) Phosphatase-Like1 (CPL1) is a biotic stress susceptibility gene.Scientific reports · 2018Article
- The over-expression of a chrysanthemum gene encoding an RNA polymerase II CTD phosphatase-like 1 enzyme enhances tolerance to heat stress.Horticulture research · 2018Article
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription and mRNA processing are regulated by phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II, which consists of tandem repeats of a Y(1)S(2)P(3)T(4)S(5)P(6)S(7) heptapeptide. Previous studies showed that members of the plant CTD phosphatase-like (CPL) protein family differentially regulate osmotic stress-responsive and abscisic acid-responsive transcription in Arabidopsis thaliana. Here we report that AtCPL1 and AtCPL2 specifically dephosphorylate Ser-5 of the CTD heptad in Arabidopsis RNA polymerase II, but not Ser-2. An N-terminal catalytic domain of CPL1, which suffices for CTD Ser-5 phosphatase activity in vitro, includes a signature DXDXT acylphosphatase motif, but lacks a breast cancer 1 CTD, which is an essential component of the fungal and metazoan Fcp1 CTD phosphatase enzymes. The CTD of CPL1, which contains two putative double-stranded RNA binding motifs, is essential for the in vivo function of CPL1 and includes a C-terminal 23-aa signal responsible for its nuclear targeting. CPL2 has a similar domain structure but contains only one double-stranded RNA binding motif. Combining mutant alleles of CPL1 and CPL2 causes synthetic lethality of the male but not the female gametes. These results indicate that CPL1 and CPL2 exemplify a unique family of CTD Ser-5-specific phosphatases with an essential role in plant growth and development.
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