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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2010-9-27
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1469-896X
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1906-16
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pubmed:dateRevised |
2011-10-3
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pubmed:meshHeading |
pubmed-meshheading:20669242-Amino Acid Sequence,
pubmed-meshheading:20669242-Animals,
pubmed-meshheading:20669242-Binding Sites,
pubmed-meshheading:20669242-Drosophila Proteins,
pubmed-meshheading:20669242-Drosophila melanogaster,
pubmed-meshheading:20669242-Humans,
pubmed-meshheading:20669242-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:20669242-Ligands,
pubmed-meshheading:20669242-Lysine,
pubmed-meshheading:20669242-Magnetic Resonance Spectroscopy,
pubmed-meshheading:20669242-Models, Molecular,
pubmed-meshheading:20669242-Molecular Sequence Data,
pubmed-meshheading:20669242-Protein Binding,
pubmed-meshheading:20669242-Protein Structure, Secondary,
pubmed-meshheading:20669242-Protein Structure, Tertiary,
pubmed-meshheading:20669242-Recombinant Proteins,
pubmed-meshheading:20669242-Repressor Proteins,
pubmed-meshheading:20669242-Sequence Homology, Amino Acid,
pubmed-meshheading:20669242-Solutions
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pubmed:year |
2010
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pubmed:articleTitle |
Structure of an atypical Tudor domain in the Drosophila Polycomblike protein.
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pubmed:affiliation |
Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstr. 1, Neuherberg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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