ArticleBMC genomics2008
RAWUL: a new ubiquitin-like domain in PRC1 ring finger proteins that unveils putative plant and worm PRC1 orthologs.
Article in BMC genomics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
57 citing papers in PubMed, 134 citations in OpenAlex.
- Phosphorylation of WDR48 by phototropins drives starch degradation to promote stomatal opening.Nature communications · 2026Article
- CRISPR gene editing of AtRING1 unravels a critical role of RAWUL domain in PRC1 repression of transcription.The Plant journal : for cell and molecular biology · 2026Article
- PRC1-mediated H2A.Zub promotes gene expression by preventing H3.1K27me1 incorporation in Arabidopsis.Genome biology · 2025Article
- Genome-Wide Analysis of the Rice PcG Gene Family and Its Involvement in Salt Response and Development.Plants (Basel, Switzerland) · 2025Article
- Characterization of DNA methylation reader proteins inGenome research · 2024Article
- LIKE HETEROCHROMATIN PROTEIN 1 (LHP1) partially inhibits the transcriptional activation of FT by MYB73 and regulates flowering in Arabidopsis.The Plant journal : for cell and molecular biology · 2024Article
- PRC1 Protein Subcomplexes Architecture: Focus on the Interplay between Distinct PCGF Subunits in Protein Interaction Networks.International journal of molecular sciences · 2024Article
- Transcript profiling of Polycomb gene family in Oryza sativa indicates their abiotic stress-specific response.Functional & integrative genomics · 2022Article
- Review
- Roles of Polycomb complexes in regulating gene expression and chromatin structure in plants.Plant communications · 2022Review
- Deorphanizing Caspase-3 and Caspase-9 Substrates In and Out of Apoptosis with Deep Substrate Profiling.ACS chemical biology · 2021Article
- Review
- H2A ubiquitination is essential for Polycomb Repressive Complex 1-mediated gene regulation in Marchantia polymorpha.Genome biology · 2021Article
- Dynamics of H3K27me3 Modification on Plant Adaptation to Environmental Cues.Plants (Basel, Switzerland) · 2021Review
- Mammalian PRC1 Complexes: Compositional Complexity and Diverse Molecular Mechanisms.International journal of molecular sciences · 2020Review
- The genetic basis for PRC1 complex diversity emerged early in animal evolution.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conservation of centromeric histone 3 interaction partners in plants.Journal of experimental botany · 2020Article
- Knowing When to Silence: Roles of Polycomb-Group Proteins in SAM Maintenance, Root Development, and Developmental Phase Transition.International journal of molecular sciences · 2020Review
- The Arabidopsis Nodulin Homeobox Factor AtNDX Interacts with AtRING1A/B and Negatively Regulates Abscisic Acid Signaling.The Plant cell · 2020Article
- Evolving Role of RING1 and YY1 Binding Protein in the Regulation of Germ-Cell-Specific Transcription.Genes · 2019Review
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPolycomb group (PcG) proteins are a set of chromatin-modifying proteins that play a key role in epigenetic gene regulation. The PcG proteins form large multiprotein complexes with different activities. The two best-characterized PcG complexes are the PcG repressive complex 1 (PRC1) and 2 (PRC2) that respectively possess histone 2A lysine 119 E3 ubiquitin ligase and histone 3 lysine 27 methyltransferase activities. While PRC2-like complexes are conserved throughout the eukaryotic kingdoms, PRC1-like complexes have only been described in Drosophila and vertebrates. Since both complexes are required for the gene silencing mechanism in Drosophila and vertebrates, how PRC1 function is realized in organisms that apparently lack PRC1 such as plants, is so far unknown. In vertebrates, PRC1 includes three proteins, Ring1B, Ring1A, and Bmi-1 that form an E3 ubiquitin ligase complex. These PRC1 proteins have an N-terminally located Ring finger domain associated to a poorly characterized conserved C-terminal region.
resultsWe obtained statistically significant evidences of sequence similarity between the C-terminal region of the PRC1 Ring finger proteins and the ubiquitin (Ubq)-like family proteins, thus defining a new Ubq-like domain, the RAWUL domain. In addition, our analysis revealed the existence of plant and worm proteins that display the conserved combination of a Ring finger domain at the N-terminus and a RAWUL domain at the C-terminus.
conclusionAnalysis of the conserved domain architecture among PRC1 Ring finger proteins revealed the existence of long sought PRC1 protein orthologs in these organisms, suggesting the functional conservation of PRC1 throughout higher eukaryotes.
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