tudor domain-containing protein 3 | Deciphering arginine methylation: Tudor tells the tale tudor domain-containing protein 3 The Tudor domain-containing protein 3 (TDRD3) is one of the major methyl .
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0 · Tudor Domain: Current Biology
1 · Tudor Domain Containing Protein 3 Promotes Tumorigenesis and
2 · TDRD3, a novel Tudor domain
3 · TDRD3 tudor domain containing 3 [ Homo sapiens (human) ]
4 · TDRD3 promotes DHX9 chromatin recruitment and R
5 · TDRD3 Gene
6 · Entry
7 · Deciphering arginine methylation: Tudor tells the tale
8 · Crystal structure of Tudor domain of TDRD3 in complex with a
9 · Arginine methylation of USP9X promotes its interaction with
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TDRD3 (Tudor Domain Containing 3) is a Protein Coding gene. Diseases . The epigenetic 'reader' Tudor domain-containing protein 3 (TDRD3), which .
We report here that TDRD3 localizes predominantly to the cytoplasm, where it co . Furthermore, TDRD3 regulates the expression of a number of key genes .Tudor domain-containing protein 3 (TDRD3) is involved in regulating transcription and . The Tudor domain-containing protein 3 (TDRD3) is one of the major methyl .
Knockdown of endogenous TDRD3 in MCF7 cells reduced ER-dependent reporter activity and . The Tudor domain core contains a conserved β-barrel structure, with an .
Tudor domain-containing proteins have been linked to chromatin regulation, pre-mRNA processing, spliceosome assembly, the RISC complex, and to germ line development through their involvement in piRNA-mediated . The tudor gene was originally discovered in Drosophila melanogaster in 1985 in a screen for maternal factors that regulate embryonic development or fertility (for a timeline, see Box 1) (Boswell and Mahowald, 1985).The Tudor protein contains 11 repeats of a domain, later termed the Tudor domain, that was subsequently found to be present in many other proteins that .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 .Tudor domain-containing protein 3 (TDRD3) are highly similar and that they both have the ability to interact with arginine-methylated polypeptides. TDRD3 has been identified among genes whose overexpression has a strong predictive value for poor prognosis of estrogen receptor-negative breast cancers, although its precise
A Tudor domain is a protein region approximately 60 amino acids in length, which folds into an SH3-like structure with a five-stranded antiparallel beta-barrel form. [1] Tudor domains can further be organized into functional units consisting of either a single Tudor domain, tandem Tudor domains, or hybrid Tudor domains consisting of two Tudor domains linked by an anti-parallel . The Tudor domain-containing proteins are characterized by their specific interactions with methylated protein motifs, including methyl-arginines and methyl-lysines. The Tudor domain-containing .
Phylogenetic analysis of the family of Agenet/Tudor proteins in the plant kingdom. a Phylogenetic analysis represented as a simplified version of the neighbor joining (NJ) tree, with 416 sequences of proteins from 31 species, from green algae to angiosperms. The tree was divided into three clades: a) the Derived clade, containing 279 sequences from 26 species, . PTHR13681:SF24 TUDOR DOMAIN-CONTAINING PROTEIN 3 1 hit; PROSITE. View protein in PROSITE; PS50304 TUDOR 1 hit; PS50030 UBA 1 hit; Pfam. View protein in Pfam; PF08585 RMI1_N_C 1 hit; PF00567 TUDOR 1 hit; PF22562 UBA_7 1 hit; SMART. View protein in SMART; SM00333 TUDOR 1 hit; SM00165 UBA 1 hit; SUPFAM. tudor domain-containing protein 3. GeneRIFs: Gene References Into Functions. Involvement of SYCP2L and TDRD3 gene variants on ovarian reserve and reproductive outcomes: a cross-sectional study. A dual-activity topoisomerase complex regulates mRNA translation and turnover. TDRD3 is an antiviral restriction factor that promotes IFN signaling .
The Tudor domain comprises a family of motifs that mediate protein-protein interactions required for various DNA-templated biological processes. . Here, we discuss novel functions of a number of Tudor-containing proteins [including Jumonji domain-containing 2A (JMJD2A), p53-binding protein 1 (53BP1), SAGA-associated factor 29 (SGF29 .
Tudor domain containing protein 3 (TDRD3) is a modular protein identified based on its ability to recognize methylated arginine motifs through its Tudor domain. We have previously shown that TDRD3 The tudor domain is traditionally associated with RNA-binding proteins. However, tudor-containing proteins have recently been demonstrated to also bind to histone marks. The tudor-like SAWADEE domain of SAWADEE HOMEODOMAIN HOMOLOGUE 1 (SHH1) binds H3K9me2 and recruits RNA polymerase IV to mediate RNA-dependent DNA methylation [19] .Another protein containing the single tudor domain is the inner nuclear membrane protein Lamin-B receptor that binds to H4K20me2 (Hirano et al., 2012). Tandem tudor domain is present in tumor suppressor p53 binding protein 1 (53BP1) in complex with methylated p53 and H4K20me2 ( Roy et al., 2010 ).
What is the Tudor domain? The Tudor domain was first identified as a segment of approximately 60 amino acids that is present in 11 repeated units in the Drosophila protein of the same name. Drosophila tudor was first identified genetically, in a large-scale screen for maternal-effect lethal mutations that affected embryonic development. Several complementation groups .TDRD5, TDRD9 and SND1 contain only one Tudor domain in both mammals and teleosts, whereas other TDRDs contain multiple Tudor domains from 2 (ECAT8) to 8 (TDRD15), respectively (Table 1, Fig. 2A). Moreover, multiple Tudor domains in a single protein might also have dierent biological functions other than as PIWI binders Tudor domain containing protein 3 (TDRD3) is a modular protein identified based on its ability to recognize methylated arginine motifs through its Tudor domain. We have previously shown.
TDRD3 (Tudor Domain Containing 3) is a Protein Coding gene. Diseases associated with TDRD3 include Fragile X Syndrome and Leukoencephalopathy, Progressive, With Ovarian Failure. Among its related pathways are Chromatin Regulation / Acetylation and Translational Control. The epigenetic 'reader' Tudor domain-containing protein 3 (TDRD3), which recognizes methylarginine marks on histones and on the C-terminal domain of RNA polymerase II, was previously shown to recruit DNA topoisomerase 3B (TOP3B) to relax negatively supercoiled DNA and prevent R-loop formation.
We report here that TDRD3 localizes predominantly to the cytoplasm, where it co-sediments with the fragile X mental retardation protein on actively translating polyribosomes. We also demonstrate that TDRD3 accumulates into stress granules (SGs) in response to various cellular stresses. Furthermore, TDRD3 regulates the expression of a number of key genes associated with promotion of breast cancer tumorigenesis and disease progression at the level of translation. Title: Tudor Domain Containing Protein 3 Promotes Tumorigenesis and Invasive Capacity of Breast Cancer Cells.Tudor domain-containing protein 3 (TDRD3) is involved in regulating transcription and translation, promoting breast cancer progression, and modulating neurodevelopment and mental health, making it a promising therapeutic target for associated diseases. The Tudor domain-containing protein 3 (TDRD3) is one of the major methyl-arginine effector molecules that recognizes methylated arginine residues on histones and the C-terminal domain of RNA.
Knockdown of endogenous TDRD3 in MCF7 cells reduced ER-dependent reporter activity and reduced expression of TFF1, NRAS (164790), and DDX5 (180630). Yang et al. (2010) concluded that TDRD3 is a methylarginine-binding protein that . The Tudor domain core contains a conserved β-barrel structure, with an aromatic cage for methyl-ligand recognition. Crystal structures of ligand-bound extended Tudor domains (eTuds) have.
Tudor Domain: Current Biology
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tudor domain-containing protein 3|Deciphering arginine methylation: Tudor tells the tale
