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Volumn 191, Issue 2, 2015, Pages 175-183

Functional insights from high resolution structures of mouse protein arginine methyltransferase 6

Author keywords

Epigenetics; Methyltransferase; PRMT6; Protein structure; S adenosyl l methionine

Indexed keywords

GUANIDINE; HISTONE H4; METAL ION; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN PRMT6; S ADENOSYLHOMOCYSTEINE; UNCLASSIFIED DRUG; PROTEIN ARGININE METHYLTRANSFERASE 6, MOUSE;

EID: 84937817318     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2015.06.017     Document Type: Article
Times cited : (23)

References (65)
  • 6
    • 81055156654 scopus 로고    scopus 로고
    • Crystal structure of the plant epigenetic protein arginine methyltransferase 10
    • Cheng Y., Frazier M., Lu F., Cao X., Redinbo M.R. Crystal structure of the plant epigenetic protein arginine methyltransferase 10. J. Mol. Biol. 2011, 414:106-122.
    • (2011) J. Mol. Biol. , vol.414 , pp. 106-122
    • Cheng, Y.1    Frazier, M.2    Lu, F.3    Cao, X.4    Redinbo, M.R.5
  • 7
    • 84907007826 scopus 로고    scopus 로고
    • Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site
    • Cura V., Troffer-Charlier N., Wurtz J.M., Bonnefond L., Cavarelli J. Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site. Acta Crystallogr. D Biol. Crystallogr. 2014, 70:2401-2412.
    • (2014) Acta Crystallogr. D Biol. Crystallogr. , vol.70 , pp. 2401-2412
    • Cura, V.1    Troffer-Charlier, N.2    Wurtz, J.M.3    Bonnefond, L.4    Cavarelli, J.5
  • 9
    • 84884799210 scopus 로고    scopus 로고
    • Automethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivity
    • Dillon M.B., Rust H.L., Thompson P.R., Mowen K.A. Automethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivity. J. Biol. Chem. 2013, 288:27872-27880.
    • (2013) J. Biol. Chem. , vol.288 , pp. 27872-27880
    • Dillon, M.B.1    Rust, H.L.2    Thompson, P.R.3    Mowen, K.A.4
  • 13
    • 84911908602 scopus 로고    scopus 로고
    • Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop
    • Feng Y., Hadjikyriacou A., Clarke S.G. Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop. J. Biol. Chem. 2014, 289:32604-32616.
    • (2014) J. Biol. Chem. , vol.289 , pp. 32604-32616
    • Feng, Y.1    Hadjikyriacou, A.2    Clarke, S.G.3
  • 14
    • 0036479327 scopus 로고    scopus 로고
    • The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity
    • Frankel A., Yadav N., Lee J., Branscombe T.L., Clarke S., Bedford M.T. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 2002, 277:3537-3543.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3537-3543
    • Frankel, A.1    Yadav, N.2    Lee, J.3    Branscombe, T.L.4    Clarke, S.5    Bedford, M.T.6
  • 15
    • 0031603283 scopus 로고    scopus 로고
    • RNA and protein interactions modulated by protein arginine methylation
    • Gary J.D., Clarke S. RNA and protein interactions modulated by protein arginine methylation. Prog. Nucleic Acid Res. Mol. Biol. 1998, 61:65-131.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 16
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999, 15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 19
    • 84896718468 scopus 로고    scopus 로고
    • Profiling substrates of protein arginine N-methyltransferase 3 with S-adenosyl-l-methionine analogues
    • Guo H., Wang R., Zheng W., Chen Y., Blum G., Deng H., Luo M. Profiling substrates of protein arginine N-methyltransferase 3 with S-adenosyl-l-methionine analogues. ACS Chem. Biol. 2014, 9:476-484.
    • (2014) ACS Chem. Biol. , vol.9 , pp. 476-484
    • Guo, H.1    Wang, R.2    Zheng, W.3    Chen, Y.4    Blum, G.5    Deng, H.6    Luo, M.7
  • 20
    • 84900408448 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats
    • Hasegawa M., Toma-Fukai S., Kim J.-D., Fukamizu A., Shimizu T. Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats. FEBS Lett. 2014, 588:1942-1948.
    • (2014) FEBS Lett. , vol.588 , pp. 1942-1948
    • Hasegawa, M.1    Toma-Fukai, S.2    Kim, J.-D.3    Fukamizu, A.4    Shimizu, T.5
  • 27
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus P.A., Diederichs K. Linking crystallographic model and data quality. Science 2012, 336:1030-1033.
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 28
    • 84865176464 scopus 로고    scopus 로고
    • Cell cycle regulation by the PRMT6 arginine methyltransferase through repression of cyclin-dependent kinase inhibitors
    • Kleinschmidt M.A., de Graaf P., van Teeffelen H.A., Timmers H.T. Cell cycle regulation by the PRMT6 arginine methyltransferase through repression of cyclin-dependent kinase inhibitors. PLoS One 2012, 7:e41446.
    • (2012) PLoS One , vol.7 , pp. e41446
    • Kleinschmidt, M.A.1    de Graaf, P.2    van Teeffelen, H.A.3    Timmers, H.T.4
  • 30
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. Sect. D Biol. Crystallogr. 2004, 60:2256-2268.
    • (2004) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 31
    • 66349099312 scopus 로고    scopus 로고
    • Delineating Anopheles gambiae coactivator associated arginine methyltransferase 1 automethylation using top-down high resolution tandem mass spectrometry
    • Kuhn P., Xu Q., Cline E., Zhang D., Ge Y., Xu W. Delineating Anopheles gambiae coactivator associated arginine methyltransferase 1 automethylation using top-down high resolution tandem mass spectrometry. Protein Sci. 2009, 18:1272-1280.
    • (2009) Protein Sci. , vol.18 , pp. 1272-1280
    • Kuhn, P.1    Xu, Q.2    Cline, E.3    Zhang, D.4    Ge, Y.5    Xu, W.6
  • 32
    • 79954611535 scopus 로고    scopus 로고
    • Automethylation of CARM1 allows coupling of transcription and mRNA splicing
    • Kuhn P., Chumanov R., Wang Y., Ge Y., Burgess R.R., Xu W. Automethylation of CARM1 allows coupling of transcription and mRNA splicing. Nucleic Acids Res. 2011, 39:2717-2726.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2717-2726
    • Kuhn, P.1    Chumanov, R.2    Wang, Y.3    Ge, Y.4    Burgess, R.R.5    Xu, W.6
  • 33
    • 44349099853 scopus 로고    scopus 로고
    • A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism
    • Lakowski T.M., Frankel A. A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism. J. Biol. Chem. 2008, 283:10015-10025.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10015-10025
    • Lakowski, T.M.1    Frankel, A.2
  • 34
    • 78649684721 scopus 로고    scopus 로고
    • Neta-substituted arginyl peptide inhibitors of protein arginine N-methyltransferases
    • Lakowski T., t Hart P., Ahern C., Martin N., Frankel A. Neta-substituted arginyl peptide inhibitors of protein arginine N-methyltransferases. ACS Chem. Biol. 2010, 5:1053-1063.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 1053-1063
    • Lakowski, T.1    t Hart, P.2    Ahern, C.3    Martin, N.4    Frankel, A.5
  • 35
    • 0017337454 scopus 로고
    • S-adenosylmethionine: protein-arginine methyltransferase. Purification and mechanism of the enzyme
    • Lee H.W., Kim S., Paik W.K. S-adenosylmethionine: protein-arginine methyltransferase. Purification and mechanism of the enzyme. Biochemistry 1977, 16:78-85.
    • (1977) Biochemistry , vol.16 , pp. 78-85
    • Lee, H.W.1    Kim, S.2    Paik, W.K.3
  • 36
    • 2542429259 scopus 로고    scopus 로고
    • PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity
    • Miranda T.B., Miranda M., Frankel A., Clarke S. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. J. Biol. Chem. 2004, 279:22902-22907.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22902-22907
    • Miranda, T.B.1    Miranda, M.2    Frankel, A.3    Clarke, S.4
  • 37
    • 25144459091 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a
    • Miranda T.B., Webb K.J., Edberg D.D., Reeves R., Clarke S. Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a. Biochem. Biophys. Res. Commun. 2005, 336:831-835.
    • (2005) Biochem. Biophys. Res. Commun. , vol.336 , pp. 831-835
    • Miranda, T.B.1    Webb, K.J.2    Edberg, D.D.3    Reeves, R.4    Clarke, S.5
  • 38
    • 84863487964 scopus 로고    scopus 로고
    • The enzymatic activity of Arabidopsis protein arginine methyltransferase 10 is essential for flowering time regulation
    • Niu L., Lu F., Zhao T., Liu C., Cao X. The enzymatic activity of Arabidopsis protein arginine methyltransferase 10 is essential for flowering time regulation. Protein Cell 2012, 3:450-459.
    • (2012) Protein Cell , vol.3 , pp. 450-459
    • Niu, L.1    Lu, F.2    Zhao, T.3    Liu, C.4    Cao, X.5
  • 39
    • 84857272686 scopus 로고    scopus 로고
    • Kinetic mechanism of protein arginine methyltransferase 6 (PRMT6)
    • Obianyo O., Thompson P.R. Kinetic mechanism of protein arginine methyltransferase 6 (PRMT6). J. Biol. Chem. 2012, 287:6062-6071.
    • (2012) J. Biol. Chem. , vol.287 , pp. 6062-6071
    • Obianyo, O.1    Thompson, P.R.2
  • 40
    • 52949145297 scopus 로고    scopus 로고
    • Kinetic mechanism of protein arginine methyltransferase 1
    • Obianyo O., Osborne T.C., Thompson P.R. Kinetic mechanism of protein arginine methyltransferase 1. Biochemistry 2008, 47:10420-10427.
    • (2008) Biochemistry , vol.47 , pp. 10420-10427
    • Obianyo, O.1    Osborne, T.C.2    Thompson, P.R.3
  • 41
    • 36248991292 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 1: positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis
    • Osborne T.C., Obianyo O., Zhang X., Cheng X., Thompson P.R. Protein arginine methyltransferase 1: positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis. Biochemistry 2007, 46:13370-13381.
    • (2007) Biochemistry , vol.46 , pp. 13370-13381
    • Osborne, T.C.1    Obianyo, O.2    Zhang, X.3    Cheng, X.4    Thompson, P.R.5
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Academic Press, New York, C.W. Carter, R.M. Sweet (Eds.)
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography 1997, 307-326. Academic Press, New York. C.W. Carter, R.M. Sweet (Eds.).
    • (1997) Macromolecular Crystallography , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 45
    • 79955079071 scopus 로고    scopus 로고
    • Mechanistic studies on transcriptional coactivator protein arginine methyltransferase 1
    • Rust H.L., Zurita-Lopez C.I., Clarke S., Thompson P.R. Mechanistic studies on transcriptional coactivator protein arginine methyltransferase 1. Biochemistry 2011, 50:3332-3345.
    • (2011) Biochemistry , vol.50 , pp. 3332-3345
    • Rust, H.L.1    Zurita-Lopez, C.I.2    Clarke, S.3    Thompson, P.R.4
  • 47
    • 37549043199 scopus 로고    scopus 로고
    • Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain
    • Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G. Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain. J. Biol. Chem. 2007, 282:36444-36453.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36444-36453
    • Sayegh, J.1    Webb, K.2    Cheng, D.3    Bedford, M.T.4    Clarke, S.G.5
  • 48
    • 84899432391 scopus 로고    scopus 로고
    • Dynamic protein ligand interactions-insights from MS
    • Schmidt C., Robinson C.V. Dynamic protein ligand interactions-insights from MS. FEBS J. 2014, 281:1950-1964.
    • (2014) FEBS J. , vol.281 , pp. 1950-1964
    • Schmidt, C.1    Robinson, C.V.2
  • 49
    • 33645238282 scopus 로고    scopus 로고
    • The AT-hook of the chromatin architectural transcription factor high mobility group A1a is arginine-methylated by protein arginine methyltransferase 6
    • Sgarra R., Lee J., Tessari M.A., Altamura S., Spolaore B., Giancotti V., Bedford M.T., Manfioletti G. The AT-hook of the chromatin architectural transcription factor high mobility group A1a is arginine-methylated by protein arginine methyltransferase 6. J. Biol. Chem. 2006, 281:3764-3772.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3764-3772
    • Sgarra, R.1    Lee, J.2    Tessari, M.A.3    Altamura, S.4    Spolaore, B.5    Giancotti, V.6    Bedford, M.T.7    Manfioletti, G.8
  • 50
    • 84880183511 scopus 로고    scopus 로고
    • Automethylation of protein arginine methyltransferase 6 (PRMT6) regulates its stability and its anti-HIV-1 activity
    • Singhroy D.N., Mesplede T., Sabbah A., Quashie P.K., Falgueyret J.P., Wainberg M.A. Automethylation of protein arginine methyltransferase 6 (PRMT6) regulates its stability and its anti-HIV-1 activity. Retrovirology 2013, 10:73.
    • (2013) Retrovirology , vol.10 , pp. 73
    • Singhroy, D.N.1    Mesplede, T.2    Sabbah, A.3    Quashie, P.K.4    Falgueyret, J.P.5    Wainberg, M.A.6
  • 51
    • 84868121626 scopus 로고    scopus 로고
    • The arginine methyltransferase PRMT6 regulates cell proliferation and senescence through transcriptional repression of tumor suppressor genes
    • Stein C., Riedl S., Ruthnick D., Notzold R.R., Bauer U.M. The arginine methyltransferase PRMT6 regulates cell proliferation and senescence through transcriptional repression of tumor suppressor genes. Nucleic Acids Res. 2012, 40:9522-9533.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 9522-9533
    • Stein, C.1    Riedl, S.2    Ruthnick, D.3    Notzold, R.R.4    Bauer, U.M.5
  • 53
    • 78349299395 scopus 로고    scopus 로고
    • Förster resonance energy transfer measurements of cofactor-dependent effects on protein arginine N-methyltransferase homodimerization
    • Thomas D., Lakowski T.M., Pak M.L., Kim J.J., Frankel A. Förster resonance energy transfer measurements of cofactor-dependent effects on protein arginine N-methyltransferase homodimerization. Protein Sci. 2010, 19:2141-2151.
    • (2010) Protein Sci. , vol.19 , pp. 2141-2151
    • Thomas, D.1    Lakowski, T.M.2    Pak, M.L.3    Kim, J.J.4    Frankel, A.5
  • 54
    • 35348916034 scopus 로고    scopus 로고
    • Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains
    • Troffer-Charlier N., Cura V., Hassenboehler P., Moras D., Cavarelli J. Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains. EMBO J. 2007, 26:4391-4401.
    • (2007) EMBO J. , vol.26 , pp. 4391-4401
    • Troffer-Charlier, N.1    Cura, V.2    Hassenboehler, P.3    Moras, D.4    Cavarelli, J.5
  • 60
    • 34247158278 scopus 로고    scopus 로고
    • Arginine methylation of the human immunodeficiency virus type 1 Tat protein by PRMT6 negatively affects Tat Interactions with both cyclin T1 and the Tat transactivation region
    • Xie B., Invernizzi C.F., Richard S., Wainberg M.A. Arginine methylation of the human immunodeficiency virus type 1 Tat protein by PRMT6 negatively affects Tat Interactions with both cyclin T1 and the Tat transactivation region. J. Virol. 2007, 81:4226-4234.
    • (2007) J. Virol. , vol.81 , pp. 4226-4234
    • Xie, B.1    Invernizzi, C.F.2    Richard, S.3    Wainberg, M.A.4
  • 63
    • 35348861410 scopus 로고    scopus 로고
    • Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase
    • Yue W.W., Hassler M., Roe S.M., Thompson-Vale V., Pearl L.H. Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase. EMBO J. 2007, 26:4402-4412.
    • (2007) EMBO J. , vol.26 , pp. 4402-4412
    • Yue, W.W.1    Hassler, M.2    Roe, S.M.3    Thompson-Vale, V.4    Pearl, L.H.5
  • 64
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides
    • Zhang X., Cheng X. Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Structure 2003, 11:509-520.
    • (2003) Structure , vol.11 , pp. 509-520
    • Zhang, X.1    Cheng, X.2
  • 65
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • Zhang X., Zhou L., Cheng X. Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. EMBO J. 2000, 19:3509-3519.
    • (2000) EMBO J. , vol.19 , pp. 3509-3519
    • Zhang, X.1    Zhou, L.2    Cheng, X.3


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