Tudor Domain Containing Protein 3 Promotes Tumorigenesis and Invasive Capacity of Breast Cancer Cells
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DOI: 10.1038/s41598-017-04955-4
Abstract: 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 localizes to cytoplasmic stress granules,… read more here.
Keywords: protein; tudor domain; breast cancer; cancer cells ... See more keywords
SETDB1 activity is globally directed by H3K14 acetylation via its Triple Tudor Domain
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DOI: 10.1101/2024.04.22.590554
Abstract: SETDB1 is a major H3K9 methyltransferase involved in heterochromatin formation and silencing of repeat elements. It contains a unique Triple Tudor Domain (3TD) which specifically binds the dual modification of H3K14ac in the presence of… read more here.
Keywords: activity globally; setdb1; h3k14 acetylation; triple tudor ... See more keywords
The TUDOR domain of SMN is an H3K79me1 histone mark reader
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DOI: 10.26508/lsa.202201752
Abstract: The survival of motor neuron (SMN) protein is depleted in spinal muscular atrophy (SMA) pathology and herein defined as the first reader of histone H3 mono-methylated on lysine 79 through its central TUDOR domain. Spinal… read more here.
Keywords: h3k79me1 histone; reader; histone; tudor domain ... See more keywords
The Tudor Domain-Containing Protein, Kotsubu (CG9925), Localizes to the Nuage and Functions in piRNA Biogenesis in D. melanogaster
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DOI: 10.3389/fmolb.2022.818302
Abstract: Silencing of transposable elements (TEs) by Piwi-interacting RNAs (piRNAs) is crucial for maintaining germline genome integrity and fertility in animals. To repress TEs, PIWI clade Argonaute proteins cooperate with several Tudor domain-containing (Tdrd) proteins at… read more here.
Keywords: containing protein; nuage; localizes nuage; domain containing ... See more keywords
Recognition of Dimethylarginine Analogues by Tandem Tudor Domain Protein Spindlin1
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DOI: 10.3390/molecules27030983
Abstract: Epigenetic readout of the combinatorial posttranslational modification comprised of trimethyllysine and asymmetric dimethylarginine (H3K4me3R8me2a) takes place via biomolecular recognition of tandem Tudor-domain-containing protein Spindlin1. Through comparative thermodynamic data and molecular dynamics simulations, we sought to… read more here.
Keywords: recognition; protein spindlin1; dimethylarginine; tandem tudor ... See more keywords