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Open Access Green as soon as Postprint is submitted to ZB.
Structure of an atypical Tudor domain in the Drosophila Polycomblike protein.
Protein Sci. 19, 1906-1916 (2010)
Post-translational modifications of histone tails are among the most prominent epigenetic marks and play a critical role in transcriptional control at the level of chromatin. The Polycomblike (Pcl) protein is part of a histone methyltransferase complex (Pcl-PRC2) responsible for high levels of histone H3 K27 trimethylation. Studies in Drosophila larvae suggest that Pcl is required for anchoring Pcl-PRC2 at target genes, but how this is achieved is unknown. Pcl comprises a Tudor domain and two PHD fingers. These domains are known to recognize methylated lysine or arginine residues and could contribute to targeting of Pcl-PRC2. Here, we report an NMR structure of the Tudor domain from Drosophila Pcl (Pcl-Tudor) and binding studies with putative ligands. Pcl-Tudor contains an atypical, incomplete aromatic cage that does not interact with known Tudor domain ligands, such as methylated lysines or arginines. Interestingly, human Pcl orthologs exhibit a complete aromatic cage, suggesting that they may recognize methylated lysines. Structural comparison with other Tudor domains suggests that Pcl-Tudor may engage in intra- or intermolecular interactions through an exposed hydrophobic surface patch.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
NMR; Polycomblike; Pcl; PRC2; Tudor; Aromatic cage; Methyllysine; sDMA; Post-translational modification; Transcriptional regulation
ISSN (print) / ISBN
0961-8368
e-ISSN
1469-896X
Journal
Protein Science
Quellenangaben
Volume: 19,
Issue: 10,
Pages: 1906-1916
Publisher
Wiley
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)