| 货号 | 14779-100ug |
| 描述 | Tudor domains (or tudor-like regions) are small protein structural motifs of ~50 amino acids related to the “Royal Family” of methyl readers, which also includes chromo, malignant brain tumor (MBT), PWWP, and Agenet-like domains.1,2 Tudor domains occur either alone, in tandem, or with other domains and are found in many proteins that are involved in RNA metabolism, germ cell development, transposon silencing, DNA damage response, histone modification, and chromatin remodeling.3 The tudor domains recognize symmetric methylated arginine or methylated lysine residues.4,5,6,7Ubiquitin-like with PHD and ring finger domains 1 (UHRF1) is a multidomain-containing nuclear protein known to bind chromatin and participate in the maintenance of DNA methylation.8,9 The SET and RING associated domain of UHRF1, also called the YDG motif, binds methyl cytosines, while trimethylated histone H3 lysine 9 (H3K9me3) and unmethylated histone H3 Arginine 2 (H3R2me0) are recognized by the tandem tudor-like domains and the PHD domain, respectively.10,11,12,13,14,15 Some evidence suggests the tandem tudor-like region and adjacent PHD domain may operate together to recognize H3K9me3.16 The combinatorial recognition of the histone tail region and hemi-methylated DNA functions to regulate gene silencing by directly interacting with DNA (cytosine-5)-methyltransferase 1.17,8,18 UHRF1 also posseses E3 ubiquitin ligase activity toward histone H3 and the tumor suppressor promyelocytic leukemia protein.13,19 Binding of UHRF1 tandem tudor-like domains to H3K9me3 is involved in heterochromatin formation and maintenance.13This protein product contains the tudor-like region of UHRF1. |
| 别名 | E3 Ubiquitin-protein Ligase UHRF1;Inverted CCAAT Box Binding Protein of 90 kDa;Nuclear Protein 95;RING Finger Protein 106;Transcription Factor ICBP90;Ubiquitin-like PHD and RING Finger Domain-containing Protein 1; |
| 供应商 | Cayman |
| 应用文献 | |
| 1.Maurer-Stroh, S.,Dickens, N.J.,Hughes-Davies, L., et al. The Tudor domain Royal Family: Tudor, plant Agenet, Chromo, PWWP and MBT domains. Trends in Biochemical Sciences 28(2), 69-74 (2003). 2.Lasko, P. Tudor domain. Current Biology 20(16), R666-R667 (2010). 3.Chen, C.,Nott, T.J.,Jin, J., et al. Deciphering arginine methylation: Tudor tells the tale. Nature Reviews.Molecular Cell Biology 12(10), 629-642 (2011). 4.Kim, J.,Daniel, J.,Espejo, A., et al. Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO reports 7(4), 397-403 (2006). 5.Huang, Y.,Fang, J.,Bedford, M.T., et al. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312, 748-751 (2006). 6.Lee, J.,Thompson, J.R.,Botuyan, M.V., et al. Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Nature Structural & Molecular Biology 15(1), 109-111 (2008). 7.Sprangers, R.,Groves, M.R.,Sinning, I., et al. High-resolution X-ray and NMR structures of the SMN tudor domain: Conformational variation in the binding site for symmetrically dimethylated arginine residues. Journal of Molecular Biology 327(2), 507-520 (2003). 8.Bostick, M.,Kim, J.K.,Estève, P.O., et al. UHRF1 plays a role in maintaining DNA methylation in mammalian cells. Science 317(5845), 1760-1764 (2007). 9.Hopfner, R.,Mousli, M.,Jeltsch, J.M., et al. ICBP90, a novel human CCAAT binding protein, involved in the regulation of topoisomerase II α expression. Cancer Research 60(1), 121-128 (2000). 10.Unoki, M.,Nishidate, T. and Nakamura, Y. ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain. Oncogene 23(46), 7601-7610 (2004). 11.Sharif, J.,Muto, M.,Takebayashi, S.i., et al. The SRA protein Np95 mediates epigenetic inheritance by recruiting Dnmt1 to methylated DNA. Nature 450(7171), 908-912 (2007). 12.Avvakumov, G.V.,Walker, J.R.,Xue, S., et al. Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1. Nature 455(7214), 822-825 (2008). 13.Karagianni, P.,Amazit, L.,Qin, J., et al. ICBP90, a novel methyl K9 H3 binding protein linking protein ubiquitination with heterochromatin formation. Molecular and Cellular Biology 28(2), 705-717 (2008). 14.Hu, L.,Li, Z.,Wang, P., et al. Crystal structure of PHD domain of UHRF1 and insights into recognition of unmodified histone H3 arginine residue 2. Cell Research 21(9), 1374-1378 (2011). 15.Lallous, N.,Legrand, P.,McEwen, A.G., et al. The PHD finger of human UHRF1 reveals a new subgroup of unmethylated histone H3 tail readers. PLoS One 6(11), e27599 (2011). 16.Xie, S.,Jakoncic, J. and Qian, C. UHRF1 double tudor domain and the adjacent PHD finger act together to recognize K9me3-containing histone H3 tail. Journal of Molecular Biology 415(2), 318-328 (2012). 17.Felle, M.,Joppien, S.,Németh, A., et al. The USP7/Dnmt1 complex stimulates the DNA methylation activity of Dnmt1 and regulates the stability of UHRF1. Nucleic Acids Research 39(19), 8355-8365 (2011). 18.Rothbart, S.B.,Krajewski, K.,Nady, N., et al. Association of UHRF1 with methylated H3K9 directs the maintenance of DNA methylation. Nature Structural & Molecular Biology 19(11), 1155-1160 (2012). 19.Guan, D.,Factor, D.,Liu, Y., et al. The epigenetic regulator UHRF1 promotes ubiquitination-mediated degradation of the tumor-suppressor protein promyelocytic leukemia protein. Oncogene 32(33), 3819-3828 (2013). | |
| 运输条件 | Dry ice in continental US; may vary elsewhere |
| 存放说明 | -80 |
| 纯度 | ≥95% estimated by SDS-PAGE |
| 稳定性 | ≥ 1 year |
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