BMC Genomics Research article RAWUL: A new ubiquitin-like domain in PRC1 Ring finger proteins that unveils putative plant and worm PRC1 orthologs Luis Sanchez-Pulido1, Damien Devos2, Zinmay R Sung3 and Myriam Calonje*4 BioMed Central Open Access Address: 1Centro Nacional de Biotecnología (CNB-CSIC). Cantoblanco, E-28049 Madrid, Spain, 2EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany, 3Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA and 4Heidelberg Institute of Plant Sciences, Department of Biodiversity and Plant Systematics, University of Heidelberg, Im Neuenheimer Feld 345, 69120 Heidelberg, Germany Email: Luis Sanchez-Pulido - sanchez@cnb.uam.es; Damien Devos - devos@embl.de; Zinmay R Sung - zrsung@nature.berkeley.edu; Myriam Calonje* - mcalonje@hip.uni-heidelberg.de * Corresponding author Published: 27 June 2008 BMC Genomics 2008, 9:308 doi:10.1186/1471-2164-9-308 This article is available from: http://www.biomedcentral.com/1471-2164/9/308 Received: 14 March 2008 Accepted: 27 June 2008 © 2008 Sanchez-Pulido et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abstract 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. Background Polycomb group (PcG) proteins are epigenetic gene regu- lators implicated in important cellular and developmen- tal processes. In animals, PcG proteins were primarily known for their role in maintaining cell identity during the establishment of the body plan [1], but recently they have also been implicated in other important processes like stem cell self-renewal and cancer [2,3]. In plants, the PcG proteins are involved in the repression of flowering during vegetative development [4,5], seed development Page 1 of 11 (page number not for citation purposes)