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Volumn 7, Issue 2, 2012, Pages

Crystal structure of TDRD3 and methyl-arginine binding characterization of TDRD3, SMN and SPF30

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BINDING PROTEIN; METHYLARGININE; SPLICING FACTOR 30; SURVIVAL MOTOR NEURON PROTEIN; TUDOR DOMAIN CONTAINING PROTEIN 3; UNCLASSIFIED DRUG; DIMETHYLARGININE; DRUG DERIVATIVE; PROTEIN; SMNDC1 PROTEIN, HUMAN; TDRD3 PROTEIN, HUMAN;

EID: 84857148540     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0030375     Document Type: Article
Times cited : (76)

References (48)
  • 1
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation an emerging regulator of protein function
    • Bedford MT, Richard S, (2005) Arginine methylation an emerging regulator of protein function. Mol Cell 18: 263-272.
    • (2005) Mol Cell , vol.18 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 2
    • 79959829510 scopus 로고    scopus 로고
    • Histone arginine methylation
    • Di Lorenzo A, Bedford MT, (2011) Histone arginine methylation. FEBS Lett 585: 2024-2031.
    • (2011) FEBS Lett , vol.585 , pp. 2024-2031
    • Di Lorenzo, A.1    Bedford, M.T.2
  • 3
    • 64749109224 scopus 로고    scopus 로고
    • Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation
    • Lee YH, Stallcup MR, (2009) Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation. Mol Endocrinol 23: 425-433.
    • (2009) Mol Endocrinol , vol.23 , pp. 425-433
    • Lee, Y.H.1    Stallcup, M.R.2
  • 4
    • 0035947239 scopus 로고    scopus 로고
    • SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets
    • Friesen WJ, Massenet S, Paushkin S, Wyce A, Dreyfuss G, (2001) SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol Cell 7: 1111-1117.
    • (2001) Mol Cell , vol.7 , pp. 1111-1117
    • Friesen, W.J.1    Massenet, S.2    Paushkin, S.3    Wyce, A.4    Dreyfuss, G.5
  • 5
    • 77950488501 scopus 로고    scopus 로고
    • How does the royal family of Tudor rule the PIWI-interacting RNA pathway?
    • Siomi MC, Mannen T, Siomi H, (2010) How does the royal family of Tudor rule the PIWI-interacting RNA pathway? Genes Dev 24: 636-646.
    • (2010) Genes Dev , vol.24 , pp. 636-646
    • Siomi, M.C.1    Mannen, T.2    Siomi, H.3
  • 6
    • 33846001366 scopus 로고    scopus 로고
    • The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing
    • Cheng D, Cote J, Shaaban S, Bedford MT, (2007) The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing. Mol Cell 25: 71-83.
    • (2007) Mol Cell , vol.25 , pp. 71-83
    • Cheng, D.1    Cote, J.2    Shaaban, S.3    Bedford, M.T.4
  • 7
    • 35349030188 scopus 로고    scopus 로고
    • Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive
    • Guccione E, Bassi C, Casadio F, Martinato F, Cesaroni M, et al. (2007) Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive. Nature 449: 933-937.
    • (2007) Nature , vol.449 , pp. 933-937
    • Guccione, E.1    Bassi, C.2    Casadio, F.3    Martinato, F.4    Cesaroni, M.5
  • 8
    • 33748949071 scopus 로고    scopus 로고
    • Structural basis for molecular recognition and presentation of histone H3 by WDR5
    • Schuetz A, Allali-Hassani A, Martin F, Loppnau P, Vedadi M, et al. (2006) Structural basis for molecular recognition and presentation of histone H3 by WDR5. EMBO J 25: 4245-4252.
    • (2006) EMBO J , vol.25 , pp. 4245-4252
    • Schuetz, A.1    Allali-Hassani, A.2    Martin, F.3    Loppnau, P.4    Vedadi, M.5
  • 9
    • 20444417108 scopus 로고    scopus 로고
    • WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development
    • Wysocka J, Swigut T, Milne TA, Dou Y, Zhang X, et al. (2005) WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development. Cell 121: 859-872.
    • (2005) Cell , vol.121 , pp. 859-872
    • Wysocka, J.1    Swigut, T.2    Milne, T.A.3    Dou, Y.4    Zhang, X.5
  • 10
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
    • Li H, Ilin S, Wang W, Duncan EM, Wysocka J, et al. (2006) Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature 442: 91-95.
    • (2006) Nature , vol.442 , pp. 91-95
    • Li, H.1    Ilin, S.2    Wang, W.3    Duncan, E.M.4    Wysocka, J.5
  • 11
    • 35348986412 scopus 로고    scopus 로고
    • Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation
    • Kirmizis A, Santos-Rosa H, Penkett CJ, Singer MA, Vermeulen M, et al. (2007) Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation. Nature 449: 928-932.
    • (2007) Nature , vol.449 , pp. 928-932
    • Kirmizis, A.1    Santos-Rosa, H.2    Penkett, C.J.3    Singer, M.A.4    Vermeulen, M.5
  • 12
    • 41249088464 scopus 로고    scopus 로고
    • Arginine methylation of the histone H3 tail impedes effector binding
    • Iberg AN, Espejo A, Cheng D, Kim D, Michaud-Levesque J, et al. (2008) Arginine methylation of the histone H3 tail impedes effector binding. J Biol Chem 283: 3006-3010.
    • (2008) J Biol Chem , vol.283 , pp. 3006-3010
    • Iberg, A.N.1    Espejo, A.2    Cheng, D.3    Kim, D.4    Michaud-Levesque, J.5
  • 14
    • 78549287139 scopus 로고    scopus 로고
    • Keeping it in the family: diverse histone recognition by conserved structural folds
    • Yap KL, Zhou MM, (2010) Keeping it in the family: diverse histone recognition by conserved structural folds. Crit Rev Biochem Mol Biol 45: 488-505.
    • (2010) Crit Rev Biochem Mol Biol , vol.45 , pp. 488-505
    • Yap, K.L.1    Zhou, M.M.2
  • 15
    • 65249151919 scopus 로고    scopus 로고
    • Structure and function of histone methylation binding proteins
    • Adams-Cioaba MA, Min J, (2009) Structure and function of histone methylation binding proteins. Biochem Cell Biol 87: 93-105.
    • (2009) Biochem Cell Biol , vol.87 , pp. 93-105
    • Adams-Cioaba, M.A.1    Min, J.2
  • 16
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM, (2006) Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312: 748-751.
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 17
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan MV, Lee J, Ward IM, Kim JE, Thompson JR, et al. (2006) Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 127: 1361-1373.
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.E.4    Thompson, J.R.5
  • 18
    • 23344444863 scopus 로고    scopus 로고
    • Tudor domains bind symmetrical dimethylated arginines
    • Cote J, Richard S, (2005) Tudor domains bind symmetrical dimethylated arginines. J Biol Chem 280: 28476-28483.
    • (2005) J Biol Chem , vol.280 , pp. 28476-28483
    • Cote, J.1    Richard, S.2
  • 19
    • 77956271553 scopus 로고    scopus 로고
    • Structural basis for methylarginine-dependent recognition of Aubergine by Tudor
    • Liu H, Wang JY, Huang Y, Li Z, Gong W, et al. (2010) Structural basis for methylarginine-dependent recognition of Aubergine by Tudor. Genes Dev.
    • (2010) Genes Dev
    • Liu, H.1    Wang, J.Y.2    Huang, Y.3    Li, Z.4    Gong, W.5
  • 20
    • 78649842259 scopus 로고    scopus 로고
    • Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain
    • Liu K, Chen C, Guo Y, Lam R, Bian C, et al. (2010) Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proc Natl Acad Sci U S A 107: 18398-18403.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 18398-18403
    • Liu, K.1    Chen, C.2    Guo, Y.3    Lam, R.4    Bian, C.5
  • 21
    • 78650233514 scopus 로고    scopus 로고
    • TDRD3 is an effector molecule for arginine-methylated histone marks
    • Yang Y, Lu Y, Espejo A, Wu J, Xu W, et al. (2010) TDRD3 is an effector molecule for arginine-methylated histone marks. Mol Cell 40: 1016-1023.
    • (2010) Mol Cell , vol.40 , pp. 1016-1023
    • Yang, Y.1    Lu, Y.2    Espejo, A.3    Wu, J.4    Xu, W.5
  • 22
    • 0037459239 scopus 로고    scopus 로고
    • High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues
    • Sprangers R, Groves MR, Sinning I, Sattler M, (2003) High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues. J Mol Biol 327: 507-520.
    • (2003) J Mol Biol , vol.327 , pp. 507-520
    • Sprangers, R.1    Groves, M.R.2    Sinning, I.3    Sattler, M.4
  • 23
    • 79953288782 scopus 로고    scopus 로고
    • The C-terminal domain of RNA polymerase II is modified by site-specific methylation
    • Sims RJ 3rd, Rojas LA, Beck D, Bonasio R, Schuller R, et al. (2011) The C-terminal domain of RNA polymerase II is modified by site-specific methylation. Science 332: 99-103.
    • (2011) Science , vol.332 , pp. 99-103
    • Sims 3rd, R.J.1    Rojas, L.A.2    Beck, D.3    Bonasio, R.4    Schuller, R.5
  • 24
    • 82955233813 scopus 로고    scopus 로고
    • Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins
    • Tripsianes K, Madl T, Machyna M, Fessas D, Englbrecht C, et al. (2011) Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins. Nat Struct Mol Biol 18: 1414-1420.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 1414-1420
    • Tripsianes, K.1    Madl, T.2    Machyna, M.3    Fessas, D.4    Englbrecht, C.5
  • 26
    • 65549091962 scopus 로고    scopus 로고
    • Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2
    • Guo Y, Nady N, Qi C, Allali-Hassani A, Zhu H, et al. (2009) Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2. Nucleic Acids Res.
    • (2009) Nucleic Acids Res
    • Guo, Y.1    Nady, N.2    Qi, C.3    Allali-Hassani, A.4    Zhu, H.5
  • 28
    • 0032567036 scopus 로고    scopus 로고
    • A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA splicing
    • Pellizzoni L, Kataoka N, Charroux B, Dreyfuss G, (1998) A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA splicing. Cell 95: 615-624.
    • (1998) Cell , vol.95 , pp. 615-624
    • Pellizzoni, L.1    Kataoka, N.2    Charroux, B.3    Dreyfuss, G.4
  • 29
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein
    • Brahms H, Meheus L, de Brabandere V, Fischer U, Luhrmann R, (2001) Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA 7: 1531-1542.
    • (2001) RNA , vol.7 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    de Brabandere, V.3    Fischer, U.4    Luhrmann, R.5
  • 30
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
    • Meister G, Eggert C, Buhler D, Brahms H, Kambach C, et al. (2001) Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr Biol 11: 1990-1994.
    • (2001) Curr Biol , vol.11 , pp. 1990-1994
    • Meister, G.1    Eggert, C.2    Buhler, D.3    Brahms, H.4    Kambach, C.5
  • 31
    • 34548356376 scopus 로고    scopus 로고
    • Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins
    • Gonsalvez GB, Tian L, Ospina JK, Boisvert FM, Lamond AI, et al. (2007) Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. J Cell Biol 178: 733-740.
    • (2007) J Cell Biol , vol.178 , pp. 733-740
    • Gonsalvez, G.B.1    Tian, L.2    Ospina, J.K.3    Boisvert, F.M.4    Lamond, A.I.5
  • 32
    • 0037073714 scopus 로고    scopus 로고
    • Determinants of the interaction of the spinal muscular atrophy disease protein SMN with the dimethylarginine-modified box H/ACA small nucleolar ribonucleoprotein GAR1
    • Whitehead SE, Jones KW, Zhang X, Cheng X, Terns RM, et al. (2002) Determinants of the interaction of the spinal muscular atrophy disease protein SMN with the dimethylarginine-modified box H/ACA small nucleolar ribonucleoprotein GAR1. J Biol Chem 277: 48087-48093.
    • (2002) J Biol Chem , vol.277 , pp. 48087-48093
    • Whitehead, S.E.1    Jones, K.W.2    Zhang, X.3    Cheng, X.4    Terns, R.M.5
  • 33
    • 0142246643 scopus 로고    scopus 로고
    • The Ewing's sarcoma protein interacts with the Tudor domain of the survival motor neuron protein
    • Young PJ, Francis JW, Lince D, Coon K, Androphy EJ, et al. (2003) The Ewing's sarcoma protein interacts with the Tudor domain of the survival motor neuron protein. Brain Res Mol Brain Res 119: 37-49.
    • (2003) Brain Res Mol Brain Res , vol.119 , pp. 37-49
    • Young, P.J.1    Francis, J.W.2    Lince, D.3    Coon, K.4    Androphy, E.J.5
  • 35
    • 79960621198 scopus 로고    scopus 로고
    • Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation
    • Bian C, Xu C, Ruan J, Lee KK, Burke TL, et al. (2011) Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation. Embo J.
    • (2011) Embo J
    • Bian, C.1    Xu, C.2    Ruan, J.3    Lee, K.K.4    Burke, T.L.5
  • 36
    • 78249286851 scopus 로고    scopus 로고
    • Structural Studies of the Tandem Tudor Domains of Fragile X Mental Retardation Related Proteins FXR1 and FXR2
    • Adams-Cioaba MA, Guo Y, Bian C, Amaya MF, Lam R, et al. (2010) Structural Studies of the Tandem Tudor Domains of Fragile X Mental Retardation Related Proteins FXR1 and FXR2. PLoS One 5: e13559.
    • (2010) PLoS One , vol.5
    • Adams-Cioaba, M.A.1    Guo, Y.2    Bian, C.3    Amaya, M.F.4    Lam, R.5
  • 37
    • 79959494918 scopus 로고    scopus 로고
    • Structural and Histone Binding Ability Characterizations of Human PWWP Domains
    • Wu H, Zeng H, Lam R, Tempel W, Amaya MF, et al. (2011) Structural and Histone Binding Ability Characterizations of Human PWWP Domains. PLoS One 6: e18919.
    • (2011) PLoS One , vol.6
    • Wu, H.1    Zeng, H.2    Lam, R.3    Tempel, W.4    Amaya, M.F.5
  • 39
    • 79952473660 scopus 로고    scopus 로고
    • The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain
    • Xu C, Bian C, Lam R, Dong A, Min J, (2011) The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain. Nat Commun 2: 227.
    • (2011) Nat Commun , vol.2 , pp. 227
    • Xu, C.1    Bian, C.2    Lam, R.3    Dong, A.4    Min, J.5
  • 43
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0
    • Bricogne G, Vonrhein C, Flensburg C, Schiltz M, Paciorek W, (2003) Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr D Biol Crystallogr 59: 2023-2030.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 45
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 47
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn MD, Murshudov GN, Papiz MZ, (2003) Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol 374: 300-321.
    • (2003) Methods Enzymol , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3


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