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Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. Additionally we are shipping TDRD3 Antibodies (22) and and many more products for this protein.
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Structural basis of the interaction between TOP3B (show TOP3B Proteins) and the TDRD3 auxiliary factor has been reported.
Top3b (show TOP3B Proteins) proteins from several animals associate with polyribosomes, which are units of mRNA translation, whereas the Top3 homologs from E. coli and yeast lack the association. The Top3b (show TOP3B Proteins)-polyribosome association requires TDRD3, which directly interacts with Top3beta and is present in animals but not bacteria or yeast.
The binding specificity and affinity of the Tudor domains of TDRD3, SMN (show STMN1 Proteins) and SPF30 (show SMNDC1 Proteins) proteins were characterized quantitatively.
The TDRD3 is an effector molecule that promotes transcription by binding methylarginine marks on histone tails.
Tudor domain of TDRD3 was required for its recruitment to cytoplasmic stress granules.
propose a contribution of Tdrd3 to FMRP (show FMR1 Proteins)-mediated translational repression and suggest that the loss of the FMRP (show FMR1 Proteins)-Tdrd3 interaction caused by the I304N mutation might contribute to the pathogenesis of Fragile X (show FMR1 Proteins) syndrome
Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In nucleus, acts as a core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine- methylated loci. In cytoplasm, may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins (By similarity).
tudor domain containing 3
, tudor domain-containing protein 3