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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References
SHOWING 1-10 OF 64 REFERENCES
Structure of an atypical Tudor domain in the Drosophila Polycomblike protein
- BiologyProtein science : a publication of the Protein Society
- 2010
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
- BiologyEMBO reports
- 2006
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.
Structure and ligand binding of the extended Tudor domain of D. melanogaster Tudor-SN.
- Chemistry, BiologyJournal of molecular biology
- 2009
Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain
- BiologyProceedings of the National Academy of Sciences
- 2010
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.
How does the royal family of Tudor rule the PIWI-interacting RNA pathway?
- BiologyGenes & development
- 2010
It was demonstrated that multiple members of the Tudor (Tud) family of proteins, which are necessary for gametogenesis in both flies and mice, associate with PIWI proteins specifically through sDMAs in various but particular combinations.
Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A
- Chemistry, BiologyScience
- 2006
This study provides mechanistic insights into recognition of methylated histone tails by tudor domains and reveals the structural intricacy of methyl-lysine recognition by two closely spaced effector domains.
A systematic analysis of Drosophila TUDOR domain‐containing proteins identifies Vreteno and the Tdrd12 family as essential primary piRNA pathway factors
- BiologyThe EMBO journal
- 2011
A critical role is demonstrated for CG4771 (Vreteno) in detail and this protein is identified as essential for the primary piRNA pathway in the germline and probably replace the function of the related but soma‐specific factor Yb.
SMN Tudor domain structure and its interaction with the Sm proteins
- Biology, ChemistryNature Structural Biology
- 2001
The three-dimensional structure of the Tudor domain of human SMN is determined and it is shown that a conserved negatively charged surface that is shown to interact with the C-terminal Arg and Gly-rich tails of Sm proteins.
TDRD3 is an effector molecule for arginine-methylated histone marks.
- BiologyMolecular cell
- 2010
Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
- BiologyNature
- 2004
The structure of the domain of 53BP1, a conserved checkpoint protein with properties of a DNA DSB sensor, is solved and it is proposed that 53 BP1 senses DSBs indirectly through changes in higher-order chromatin structure that expose the 53BP 1 binding site.