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Volumn 586, Issue 13, 2012, Pages 1783-1789

PHD finger of the SUMO ligase Siz/PIAS family in rice reveals specific binding for methylated histone H3 at lysine 4 and arginine 2

Author keywords

Methylated histone H3; NMR structure; PHD finger; Protein peptide interaction; SUMO ligase Siz PIAS

Indexed keywords

ARGININE; HISTONE H3; LIGASE; LYSINE; PROTEIN INHIBITOR OF ACTIVATED STAT; SUMO LIGASE; UNCLASSIFIED DRUG;

EID: 84862503634     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.04.063     Document Type: Article
Times cited : (11)

References (53)
  • 1
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay, R.T. (2005) SUMO: a history of modification. Mol. Cell 18, 1-12.
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 2
    • 34250214907 scopus 로고    scopus 로고
    • SUMOrganization of the nucleus
    • Heun, P. (2007) SUMOrganization of the nucleus. Curr. Opin. Cell Biol. 19, 350-355.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 350-355
    • Heun, P.1
  • 3
    • 0346100493 scopus 로고    scopus 로고
    • PIAS/SUMO: New partners in transcriptional regulation
    • DOI 10.1007/s00018-003-3129-1
    • Schmidt, D. and Müller, S. (2003) PIAS/SUMO: new partners in transcriptional regulation. Cell. Mol. Life Sci. 60, 2561-2574. (Pubitemid 38041360)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.12 , pp. 2561-2574
    • Schmidt, D.1    Muller, S.2
  • 4
  • 5
    • 23444461182 scopus 로고    scopus 로고
    • Regulation of gene-activation pathways by pias proteins in the immune system
    • DOI 10.1038/nri1667
    • Shuai, K. and Liu, B. (2005) Regulation of gene-activation pathway by PIA proteins in the immune system. Nat. Rev. Immunol. 5, 593-605. (Pubitemid 41113191)
    • (2005) Nature Reviews Immunology , vol.5 , Issue.8 , pp. 593-605
    • Shuai, K.1    Liu, B.2
  • 8
    • 77952566949 scopus 로고    scopus 로고
    • Mechanisms, regulation and consequences of protein SUMOylation
    • Wilkinson, K.A. and Henley, J.M. (2010) Mechanisms, regulation and consequences of protein SUMOylation. Biochem. J. 428, 133-145.
    • (2010) Biochem. J. , vol.428 , pp. 133-145
    • Wilkinson, K.A.1    Henley, J.M.2
  • 9
    • 77950865637 scopus 로고    scopus 로고
    • Sumoylation and other ubiquitin-like post-translational modifications in plants
    • Miura, K. and Hasegawa, M.P. (2010) Sumoylation and other ubiquitin-like post-translational modifications in plants. Trends Cell Biol. 20, 223-232.
    • (2010) Trends Cell Biol. , vol.20 , pp. 223-232
    • Miura, K.1    Hasegawa, M.P.2
  • 12
    • 69249203574 scopus 로고    scopus 로고
    • SUMO association with repressor complexes, emerging routes for transcriptional control
    • Garcia-Dominguez, M. and Reyes, J.C. (2009) SUMO association with repressor complexes, emerging routes for transcriptional control. Biochim. Biophys. Acta 1789, 451-459.
    • (2009) Biochim. Biophys. Acta , vol.1789 , pp. 451-459
    • Garcia-Dominguez, M.1    Reyes, J.C.2
  • 13
    • 73449092854 scopus 로고    scopus 로고
    • SUMO engages multiple corepressors to regulate chromatin structure and transcription
    • Ouyang, J. and Gill, G. (2009) SUMO engages multiple corepressors to regulate chromatin structure and transcription. Epigenetics 4, 440-444.
    • (2009) Epigenetics , vol.4 , pp. 440-444
    • Ouyang, J.1    Gill, G.2
  • 14
    • 0035863152 scopus 로고    scopus 로고
    • Solution structure of the PHD domain from the KAP-1 corepressor: Structural determinants for PHD, RING and LIM zinc-binding domains
    • DOI 10.1093/emboj/20.1.165
    • Capili, A.D., Schultz, D.C., Rauscher III, F.J. and Borden, L.B. (2001) Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains. EMBO J. 20, 165-177. (Pubitemid 32099113)
    • (2001) EMBO Journal , vol.20 , Issue.1-2 , pp. 165-177
    • Capili, A.D.1    Schultz, D.C.2    Rauscher, F.J.3    Borden, K.L.B.4
  • 15
    • 30944452960 scopus 로고    scopus 로고
    • The PHD finger, a nuclear protein-interaction domain
    • Bienz, M. (2006) The PHD finger, a nuclear protein-interaction domain. Trends Biochem. Sci. 31, 35-40.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 35-40
    • Bienz, M.1
  • 16
    • 0027630839 scopus 로고
    • HAT3.1, a novel Arabidopsis homeodomain protein containing a conserved cystein-rich region
    • Schindler, U., Beckmann, H. and Cashmore, A.R. (1993) HAT3.1, a novel Arabidopsis homeodomain protein containing a conserved cystein-rich region. Plant J. 4, 137-150.
    • (1993) Plant J. , vol.4 , pp. 137-150
    • Schindler, U.1    Beckmann, H.2    Cashmore, A.R.3
  • 17
    • 33745818717 scopus 로고    scopus 로고
    • Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2
    • DOI 10.1038/nature04814, PII NATURE04814
    • Pena, P.V., Davrazou, F., Shi, X., Walter, K.L., Verkhusha, V.V., Gozani, O., Zhao, R. and Kutateladze, T.G. (2006) Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 442, 100-103. (Pubitemid 44064217)
    • (2006) Nature , vol.442 , Issue.7098 , pp. 100-103
    • Pena, P.V.1    Davrazou, F.2    Shi, X.3    Walter, K.L.4    Verkhusha, V.V.5    Gozani, O.6    Zhao, R.7    Kutateladze, T.G.8
  • 18
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
    • DOI 10.1038/nature04802, PII NATURE04802
    • Li, H., Ilin, S., Wang, W., Duncan, E.M., Wysocka, J., Allis, C.D. and Patel, D.J. (2006) Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature 442, 91-95. (Pubitemid 44064215)
    • (2006) Nature , vol.442 , Issue.7098 , pp. 91-95
    • Li, H.1    Ilin, S.2    Wang, W.3    Duncan, E.M.4    Wysocka, J.5    Allis, C.D.6    Patel, D.J.7
  • 19
    • 33745713437 scopus 로고    scopus 로고
    • It takes a PHD to read the histone code
    • Mellor, J. (2006) It takes a PHD to read the histone code. Cell 126, 22-24.
    • (2006) Cell , vol.126 , pp. 22-24
    • Mellor, J.1
  • 20
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: Lessons from professional pocket pickers
    • DOI 10.1038/nsmb1338, PII NSMB1338
    • Taverna, S.D., Li, H., Ruthenburg, A.J., Allis, C.D. and Patel, D.J. (2007) How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Nat. Struct. Mol. Biol. 14, 1025-1040. (Pubitemid 350060344)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.11 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 21
    • 0031933143 scopus 로고    scopus 로고
    • Determining the structures of large proteins and protein complexes by NMR
    • DOI 10.1016/S0167-7799(97)01135-9
    • Clore, G.M. and Gronenborn, A.M. (1998) Determining the structure of large proteins and protein complexes by NMR. Trends Biotechnol. 16, 22-34. (Pubitemid 28064815)
    • (1998) Trends in Biotechnology , vol.16 , Issue.1 , pp. 22-34
    • Clore, G.M.1    Gronenborn, A.M.2
  • 22
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax, A. and Grzesiek, S. (1993) Methodological advances in protein NMR. Acc. Chem. Res. 26, 131-138.
    • (1993) Acc. Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 24
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 25
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen, Y., Delaglio, F., Cornilescu, G. and Bax, A. (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 44, 213-223.
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 26
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structural calculation with the new program DYANA
    • Günter, P., Mumenthaler, C. and Wüthrich, K. (1997) Torsion angle dynamics for NMR structural calculation with the new program DYANA. J. Mol. Biol. 273, 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Günter, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 27
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi, R., Billeter, M. and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55. (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 29
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • DOI 10.1021/ja026939x
    • Dominhuez, C., Boelens, R. and Bonvin, A.M.J.J. (2003) HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125, 1731-1737. (Pubitemid 36232568)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.7 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 32
    • 66249141300 scopus 로고    scopus 로고
    • The solution structure of the first PHD finger of autoimmune regulator in complex with non-modified histone H3 tail reveals the antagonistic role of H3R2 methylation
    • Chignola, F., Gaetani, M., Rebane, A., Org, T., Mollica, L., Zucchelli, C., Spitaleri, A., Mannella, V., Peterson, P. and Musco, G. (2009) The solution structure of the first PHD finger of autoimmune regulator in complex with non-modified histone H3 tail reveals the antagonistic role of H3R2 methylation. Nucl. Acid Res. 37, 2951-2961.
    • (2009) Nucl. Acid Res. , vol.37 , pp. 2951-2961
    • Chignola, F.1    Gaetani, M.2    Rebane, A.3    Org, T.4    Mollica, L.5    Zucchelli, C.6    Spitaleri, A.7    Mannella, V.8    Peterson, P.9    Musco, G.10
  • 35
    • 52049096640 scopus 로고    scopus 로고
    • The PHD domain of plant PIAS proteins mediates sumoylation of bromodomain GTE proteins
    • Garcia-Dominguez, M., March-Diaz, R. and Reyes, J.C. (2008) The PHD domain of plant PIAS proteins mediates sumoylation of bromodomain GTE proteins. J. Biol. Chem. 283, 21469-213477.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21469-213477
    • Garcia-Dominguez, M.1    March-Diaz, R.2    Reyes, J.C.3
  • 38
    • 79959829510 scopus 로고    scopus 로고
    • Histone arginine methylation
    • Di Lorenzo, A. and Bedford, M.T. (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
  • 41
    • 60549108739 scopus 로고    scopus 로고
    • Regulation of Set9-mediated H4K20 methylation by a PWWP domain protein
    • Wang, Y., Reddy, B., Thompson, J., Wang, H., Noma, K., Yates III, J.R. and Jia, S. (2009) Regulation of Set9-mediated H4K20 methylation by a PWWP domain protein. Mol. Cell 33, 428-437.
    • (2009) Mol. Cell , vol.33 , pp. 428-437
    • Wang, Y.1    Reddy, B.2    Thompson, J.3    Wang, H.4    Noma, K.5    Yates III, J.R.6    Jia, S.7
  • 44
    • 24944528328 scopus 로고    scopus 로고
    • SUMO modification is involved in the maintenance of heterochromatin stability in fission yeast
    • DOI 10.1016/j.molcel.2005.08.021, PII S1097276505015637
    • Shin, J.A., Choi, E.S., Kim, H.S., Ho, J.C.Y., Watts, F.Z., Park, S.D. and Jang, Y.K. (2005) SUMO modification is involved in the maintenance of heterochromatin stability in fission yeast. Mol. Cell 19, 817-828. (Pubitemid 41316675)
    • (2005) Molecular Cell , vol.19 , Issue.6 , pp. 817-828
    • Shin, J.A.1    Eun, S.C.2    Hyun, S.K.3    Ho, J.C.Y.4    Watts, F.Z.5    Sang, D.P.6    Jang, Y.K.7
  • 45
    • 33750447586 scopus 로고    scopus 로고
    • The Mechanisms of PML-Nuclear Body Formation
    • DOI 10.1016/j.molcel.2006.09.013, PII S1097276506006617
    • Shen, T.H., Lin, H.-K., Scaglioni, P.P., Yung, T.M. and Pandolfi, P.P. (2006) The mechanisms of PML-nuclear body formation. Mol. Cell 24, 331-339. (Pubitemid 44647906)
    • (2006) Molecular Cell , vol.24 , Issue.3 , pp. 331-339
    • Shen, T.H.1    Lin, H.-K.2    Scaglioni, P.P.3    Yung, T.M.4    Pandolfi, P.P.5
  • 46
  • 47
    • 66149091527 scopus 로고    scopus 로고
    • Solution structures and DNA binding properties of the N-terminal SAP domains of SUMO E3 ligases from Saccharomyces cerevisiae and Oryza sativa
    • Suzuki, R., Shindo, H., Tase, A., Kikuchi, Y., Shimizu, M. and Yamazaki, T. (2008) Solution structures and DNA binding properties of the N-terminal SAP domains of SUMO E3 ligases from Saccharomyces cerevisiae and Oryza sativa. Proteins 75, 336-347.
    • (2008) Proteins , vol.75 , pp. 336-347
    • Suzuki, R.1    Shindo, H.2    Tase, A.3    Kikuchi, Y.4    Shimizu, M.5    Yamazaki, T.6
  • 49
    • 0036176982 scopus 로고    scopus 로고
    • The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNAbinding folds
    • Qiu, C., Sawada, K., Zhang, X. and Cheng, X. (2002) The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNAbinding folds. Nat. Struc. Biol. 9, 217-223.
    • (2002) Nat. Struc. Biol. , vol.9 , pp. 217-223
    • Qiu, C.1    Sawada, K.2    Zhang, X.3    Cheng, X.4
  • 50
    • 31344446959 scopus 로고    scopus 로고
    • High resolution structure of the HDGF PWWP domain: A potential DNA binding domain
    • DOI 10.1110/ps.051751706
    • Lukasik, S.M., Cierpicki, T., Borloz, M., Grembecka, J., Everett, A. and Bushweller, J.H. (2006) High resolution structure of the HDGF PWWP domain: a potential DNA binding domain. Protein Sci. 15, 314-323. (Pubitemid 43145003)
    • (2006) Protein Science , vol.15 , Issue.2 , pp. 314-323
    • Lukasik, S.M.1    Cierpicki, T.2    Borloz, M.3    Grembecka, J.4    Everett, A.5    Bushweller, J.H.6
  • 51
    • 84863230348 scopus 로고    scopus 로고
    • Solution structure of Pdp1 PWWP domain reveals its unique binding sites for methylated H4K20 and DNA
    • Qiu, Y., Zhang, W., Zhao, C., Wang, Y., Wang, W., Zhang, J., Zhang, Z., Li, G., Shi, Y., Tu, X. and Wu, J. (2012) Solution structure of Pdp1 PWWP domain reveals its unique binding sites for methylated H4K20 and DNA. Biochem. J. 442, 527-538.
    • (2012) Biochem. J. , vol.442 , pp. 527-538
    • Qiu, Y.1    Zhang, W.2    Zhao, C.3    Wang, Y.4    Wang, W.5    Zhang, J.6    Zhang, Z.7    Li, G.8    Shi, Y.9    Tu, X.10    Wu, J.11
  • 52
    • 77951977878 scopus 로고    scopus 로고
    • Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1
    • Huntly, B.J.P., Göttgens, B. and Bycroft, M. (2010) Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1. Nat. Struc. Mol. Biol. 17, 617-619.
    • (2010) Nat. Struc. Mol. Biol. , vol.17 , pp. 617-619
    • Huntly, B.J.P.1    Göttgens, B.2    Bycroft, M.3
  • 53
    • 79953183354 scopus 로고    scopus 로고
    • The dynamics and mechanism of SUMO chain deconjugation by SUMOspecific proteases
    • Bekes, M., Prudden, J., Srikumar, T., Raught, B., Boddy, M.N. and Salvesen, G.S. (2011) The dynamics and mechanism of SUMO chain deconjugation by SUMOspecific proteases. J. Biol. Chem. 286, 10238-10247.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10238-10247
    • Bekes, M.1    Prudden, J.2    Srikumar, T.3    Raught, B.4    Boddy, M.N.5    Salvesen, G.S.6


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