Tudor domain‐containing proteins of Drosophila melanogaster

@article{Ying2012TudorDP,
  title={Tudor domain‐containing proteins of Drosophila melanogaster},
  author={Muying Ying and Dahua Chen},
  journal={Development},
  year={2012},
  volume={54}
}
Tudor domain‐containing proteins (Tudor proteins), which recognize and bind to methyl‐arginine/lysine residues, play important roles in diverse epigenetics, gene expression and the regulation of various small RNAs. Using the complete set of 23 Tudor proteins from Drosophila, together with the available functional information, we propose a putative link for different types of Tudor domains (histone‐binding, SMN and SND1) and the four functional groups of Tudor proteins (Group 1, binding the… 
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TLDR
An NMR structure of the Tudor domain from Drosophila Pcl (Pcl‐Tudor) is reported andStructural comparison with other Tudor domains suggests that Pcl‐tudor may engage in intra‐ or intermolecular interactions through an exposed hydrophobic surface patch, suggesting that they may recognize methylated lysines.
Tudor, MBT and chromo domains gauge the degree of lysine methylation
TLDR
These studies expose tudor and MBT domains as new classes of methyl‐lysine‐binding protein modules, and demonstrates that protein‐domain microarrays are powerful tools for the identification of new domain types that recognize histone modifications.
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TLDR
It is found that human SND1 binds PIWIL1 in an arginine methylation-dependent manner with a preference for symmetrical dimethylarginine via an aromatic cage and conserved hydrogen bonds, and provides a general paradigm for the binding mechanisms of methylarginined peptides by extended Tudor domains.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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