共查询到20条相似文献,搜索用时 31 毫秒
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Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha 总被引:1,自引:0,他引:1
Qi C Chang J Zhu Y Yeldandi AV Rao SM Zhu YJ 《The Journal of biological chemistry》2002,277(32):28624-28630
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Koh SS Li H Lee YH Widelitz RB Chuong CM Stallcup MR 《The Journal of biological chemistry》2002,277(29):26031-26035
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Na-zi Lei Xiao-yan Zhang Hang-zi Chen Yuan Wang Yan-yan Zhan Zhong-hui Zheng Yue-mao Shen Qiao Wu 《Nucleic acids research》2009,37(3):832-848
PRMT1, an arginine methyltransferase, plays an important role in numerous cellular processes. In this study, we demonstrate a feedback regulatory loop between PRMT1 and the orphan receptor TR3. Unlike another orphan receptor HNF4, TR3 is not methylated by PRMT1 although they physically interact with each other. By delaying the TR3 protein degradation, PRMT1 binding leads to the elevation of TR3 cellular protein level, thereby enhances the DNA binding and transactivation activity of TR3 in a non-methyltransferase manner. Another coactivator SRC-2 acts synergistically with PRMT1 to regulate TR3 functions. In turn, TR3 binding to the catalytic domain of PRMT1 causes an inhibition of the PRMT1 methyltransferase activity. This repression results in the functional changes in some of PRMT1 substrates, including STAT3 and Sam68. The negative regulation of PRMT1 by TR3 was further confirmed in both TR3-knockdown cells and TR3-knockout mice with the use of an agonist for TR3. Taken together, our study not only identifies a regulatory role of PRMT1, independent on methyltransferase activity, in TR3 transactivation, but also characterizes a novel function of TR3 in the repression of PRMT1 methyltransferase activity. 相似文献
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Teyssier C Ou CY Khetchoumian K Losson R Stallcup MR 《Molecular endocrinology (Baltimore, Md.)》2006,20(6):1276-1286
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Mansure JJ Furtado DR de Oliveira FM Rumjanek FD Franco GR Fantappié MR 《Biochemical and biophysical research communications》2005,335(4):1163-1172
The most studied arginine methyltransferase is the type I enzyme, which catalyzes the transfer of an S-adenosyl-L-methionine to a broad spectrum of substrates, including histones, RNA-transporting proteins, and nuclear hormone receptor coactivators. We cloned a cDNA encoding a protein arginine methyltransferase in Schistosoma mansoni (SmPRMT1). SmPRMT1 is highly homologous to the vertebrate PRMT1 enzyme. In vitro methylation assays showed that SmPRMT1 recombinant protein was able to specifically methylate histone H4. Two schistosome proteins likely to be involved in RNA metabolism, SMYB1 and SmSmD3, that display a number of RGG motifs, were strongly methylated by SmPRMT1. In vitro GST pull-down assays showed that SMYB1 and SmSmD3 physically interacted with SmPRMT1. Additional GST pull-down assay suggested the occurrence of a ternary complex including SmPRMT1, SmRXR1 nuclear receptor, and the p160 (SRC-1) nuclear receptor coactivator. Together, these data suggest a mechanism by which SmPRMT1 plays a role in nuclear receptor-mediated chromatin remodeling and RNA transactions. 相似文献
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A Siarheyeva G Senisterra A Allali-Hassani A Dong E Dobrovetsky GA Wasney I Chau R Marcellus T Hajian F Liu I Korboukh D Smil Y Bolshan J Min H Wu H Zeng P Loppnau G Poda C Griffin A Aman PJ Brown J Jin R Al-Awar CH Arrowsmith M Schapira M Vedadi 《Structure (London, England : 1993)》2012,20(8):1425-1435
PRMT3, a protein arginine methyltransferase, has been shown to influence ribosomal biosynthesis by catalyzing the dimethylation of the 40S ribosomal protein S2. Although PRMT3 has been reported to be a cytosolic protein, it has been shown to methylate histone H4 peptide (H4 1-24) in?vitro. Here, we?report the identification of a PRMT3 inhibitor (1-(benzo[d][1,2,3]thiadiazol-6-yl)-3-(2-cyclohexenylethyl)urea; compound 1) with IC(50) value of 2.5?μM by screening a library of 16,000 compounds using H4 (1-24) peptide as a substrate. The crystal structure of PRMT3 in complex with compound 1 as well as kinetic analysis reveals an allosteric mechanism of inhibition. Mutating PRMT3 residues within the allosteric site or using compound 1 analogs that disrupt interactions with allosteric site residues both abrogated binding and inhibitory activity. These data demonstrate an allosteric mechanism for inhibition of protein arginine methyltransferases, an emerging class of therapeutic targets. 相似文献
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FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues
Cook JR Lee JH Yang ZH Krause CD Herth N Hoffmann R Pestka S 《Biochemical and biophysical research communications》2006,342(2):472-481
We have identified a protein, FLJ12673 or FBXO11, that contains domains characteristically present in protein arginine methyltransferases (PRMTs). Immuno-purified protein expressed from one of the four splice variants in HeLa cells and in Escherichia coli exhibited methyltransferase activity. Monomethylarginine, symmetric, and asymmetric dimethylarginine (SDMA, ADMA) were formed on arginine residues. Accordingly, we have designated the protein PRMT9. PRMT9 is the third member of the PRMT family that forms SDMA modifications in proteins. Structurally, this protein is distinct from all other known PRMTs implying that convergent evolution allowed this protein to develop the ability to methylate arginine residues and evolved elements conserved in PRMTs to accomplish this. 相似文献