We are analyzing https://link.springer.com/article/10.1186/1471-2164-9-308.

Title:
RAWUL: A new ubiquitin-like domain in PRC1 Ring finger proteins that unveils putative plant and worm PRC1 orthologs | BMC Genomics
Description:
Background Polycomb 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. Results We 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. Conclusion Analysis 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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Keywords {🔍}

pubmed, article, domain, proteins, google, scholar, cas, prc, ring, protein, finger, sequence, ubiquitin, figure, family, rawul, polycomb, conserved, biol, plant, complex, cell, central, histone, ubqlike, structure, analysis, drosophila, cterminal, group, gene, bmi, arabidopsis, human, zhang, plants, profile, domains, mol, complexes, ligase, wdrp, ringb, ubiquitination, function, pcg, region, genes, ubx, fold,

Topics {✒️}

profile-profile comparisons e-values open access article sex combs extra n-terminal ring finger significant e-values connected article download pdf histone post-translational modifications mes-2/mes-3/mes-6 complex profile-profile comparisons linked full size image x-ray crystal structure human switch/sucrose nonfermentable aaa atpase p97/vcp pcg-mediated gene repression profile-based neural networks posterior sex combs n-terminal ring domain article sanchez-pulido c-terminal conserved regions conserved c-terminal regions e3-ligase related function isolated c-terminal domain hmm-hmm comparison mammalian bmi-1 proto-oncogene eu grant 3d-repertoire conserved c-terminal region profile search direction mediate protein-protein interaction wd40 repeat domain cell cycle regulation rna-binding proteins sop-2 polycomb-group silencing major p97-cofactor involved c-terminal rawul domain c-terminal domain rawul wdr48-p80 protein family human wdr48-p80 protein human ubiquitin-specific proteases prc1 ring finger e3 ligase activity e3-ligase activity polycomb group proteins e3 ligase complex gene silencing mechanism ring finger proteins structure-based sequence alignments ring-ring complex de los paños ring finger domain ring-finger domain

Questions {❓}

Bronner C, Achour M, Arima Y, Chataigneau T, Saya H, Schini-Kerth VB: The UHRF family: Oncogenes that are drugable targets for cancer therapy in the near future?
Jentsch S, Pyrowolakis G: Ubiquitin and its kin: how close are the family ties?
Satijn DP, Otte AP: Polycomb group protein complexes: do different complexes regulate distinct target genes?

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         description:Polycomb 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. We 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. Analysis 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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      description:Polycomb 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. We 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. Analysis 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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         Domain Architecture
         WD40 Repeat
         Ring Finger Protein
         Ring Finger Domain
         Life Sciences
         general
         Microarrays
         Proteomics
         Animal Genetics and Genomics
         Microbial Genetics and Genomics
         Plant Genetics and Genomics
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      affiliation:
            name:EMBL
            address:
               name:EMBL, Heidelberg, Germany
               type:PostalAddress
            type:Organization
      name:Zinmay R Sung
      affiliation:
            name:University of California
            address:
               name:Department of Plant and Microbial Biology, University of California, Berkeley, USA
               type:PostalAddress
            type:Organization
      name:Myriam Calonje
      affiliation:
            name:University of Heidelberg
            address:
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      name:Heidelberg Institute of Plant Sciences, Department of Biodiversity and Plant Systematics, University of Heidelberg, Heidelberg, Germany

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