메뉴 건너뛰기




Volumn 289, Issue 8, 2014, Pages 4882-4895

Retinoblastoma-binding protein 1 has an interdigitated double tudor domain with DNA binding activity

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

EID: 84894427016     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.501940     Document Type: Article
Times cited : (19)

References (53)
  • 2
    • 51749123590 scopus 로고    scopus 로고
    • Identification of chromatin remodeling genes Arid4a and Arid4b as leukemia suppressor genes
    • Wu, M. Y., Eldin, K. W., and Beaudet, A. L. (2008) Identification of chromatin remodeling genes Arid4a and Arid4b as leukemia suppressor genes. J. Natl. Cancer Inst. 100, 1247-1259
    • (2008) J. Natl. Cancer Inst. , vol.100 , pp. 1247-1259
    • Wu, M.Y.1    Eldin, K.W.2    Beaudet, A.L.3
  • 3
    • 0347723868 scopus 로고    scopus 로고
    • Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription
    • Meehan, W. J., Samant, R. S., Hopper, J. E., Carrozza, M. J., Shevde, L. A., Workman, J. L., Eckert, K. A., Verderame, M. F., and Welch, D. R. (2004) Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription. J. Biol. Chem. 279, 1562-1569
    • (2004) J. Biol. Chem. , vol.279 , pp. 1562-1569
    • Meehan, W.J.1    Samant, R.S.2    Hopper, J.E.3    Carrozza, M.J.4    Shevde, L.A.5    Workman, J.L.6    Eckert, K.A.7    Verderame, M.F.8    Welch, D.R.9
  • 4
    • 0038642016 scopus 로고    scopus 로고
    • Identification and characterization of three new components of the mSin3A corepressor complex
    • Fleischer, T. C., Yun, U. J., and Ayer, D. E. (2003) Identification and characterization of three new components of the mSin3A corepressor complex. Mol. Cell Biol. 23, 3456-3467
    • (2003) Mol. Cell Biol. , vol.23 , pp. 3456-3467
    • Fleischer, T.C.1    Yun, U.J.2    Ayer, D.E.3
  • 6
    • 0035421508 scopus 로고    scopus 로고
    • RBP1L1, a retinoblastoma-binding protein-related gene encoding an antigenic epitope abundantly expressed in human carcinomas and normal testis
    • Cao, J., Gao, T., Stanbridge, E. J., and Irie, R. (2001) RBP1L1, a retinoblastoma-binding protein-related gene encoding an antigenic epitope abundantly expressed in human carcinomas and normal testis. J. Natl. Cancer Inst. 93, 1159-1165
    • (2001) J. Natl. Cancer Inst. , vol.93 , pp. 1159-1165
    • Cao, J.1    Gao, T.2    Stanbridge, E.J.3    Irie, R.4
  • 7
    • 0033602457 scopus 로고    scopus 로고
    • RBP1 induces growth arrest by repression of E2F-dependent transcription
    • Lai, A., Marcellus, R. C., Corbeil, H. B., and Branton, P. E. (1999) RBP1 induces growth arrest by repression of E2F-dependent transcription. Oncogene 18, 2091-2100
    • (1999) Oncogene , vol.18 , pp. 2091-2100
    • Lai, A.1    Marcellus, R.C.2    Corbeil, H.B.3    Branton, P.E.4
  • 9
    • 0032855532 scopus 로고    scopus 로고
    • Cytotoxic T lymphocytes that recognize decameric peptide sequences of retinoblastoma binding protein 1 (RBP-1) associated with human breast cancer
    • Takahashi, T., Cao, J., Hoon, D. S., and Irie, R. F. (1999) Cytotoxic T lymphocytes that recognize decameric peptide sequences of retinoblastoma binding protein 1 (RBP-1) associated with human breast cancer. Br. J. Cancer 81, 342-349
    • (1999) Br. J. Cancer , vol.81 , pp. 342-349
    • Takahashi, T.1    Cao, J.2    Hoon, D.S.3    Irie, R.F.4
  • 11
    • 33751086773 scopus 로고    scopus 로고
    • Deficiency of Rbbp1/ Arid4a and Rbbp1l1/Arid4b alters epigenetic modifications and suppresses an imprinting defect in the PWS/AS domain
    • Wu, M. Y., Tsai, T. F., and Beaudet, A. L. (2006) Deficiency of Rbbp1/ Arid4a and Rbbp1l1/Arid4b alters epigenetic modifications and suppresses an imprinting defect in the PWS/AS domain. Genes Dev. 20, 2859-2870
    • (2006) Genes Dev. , vol.20 , pp. 2859-2870
    • Wu, M.Y.1    Tsai, T.F.2    Beaudet, A.L.3
  • 13
    • 84863277661 scopus 로고    scopus 로고
    • Structural insight into recognition of methylated histone tails by retinoblastoma-binding protein 1
    • Gong, W., Zhou, T., Mo, J., Perrett, S., Wang, J., and Feng, Y. (2012) Structural insight into recognition of methylated histone tails by retinoblastoma-binding protein 1. J. Biol. Chem. 287, 8531-8540
    • (2012) J. Biol. Chem. , vol.287 , pp. 8531-8540
    • Gong, W.1    Zhou, T.2    Mo, J.3    Perrett, S.4    Wang, J.5    Feng, Y.6
  • 14
    • 13744250058 scopus 로고    scopus 로고
    • DNA-binding properties of ARID family proteins
    • Patsialou, A., Wilsker, D., and Moran, E. (2005) DNA-binding properties of ARID family proteins. Nucleic Acids Res. 33, 66-80
    • (2005) Nucleic Acids Res. , vol.33 , pp. 66-80
    • Patsialou, A.1    Wilsker, D.2    Moran, E.3
  • 15
    • 0031081575 scopus 로고    scopus 로고
    • Tudor domains in proteins that interact with RNA
    • Ponting, C. P. (1997) Tudor domains in proteins that interact with RNA. Trends Biochem. Sci. 22, 51-52
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 51-52
    • Ponting, C.P.1
  • 16
    • 0031027360 scopus 로고    scopus 로고
    • The human EBNA-2 coactivator p100. Multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development
    • Callebaut, I., and Mornon, J. P. (1997) The human EBNA-2 coactivator p100. Multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development. Biochem. J. 321, 125-132
    • (1997) Biochem. J. , vol.321 , pp. 125-132
    • Callebaut, I.1    Mornon, J.P.2
  • 18
    • 84861980264 scopus 로고    scopus 로고
    • Tudor domain proteins in development
    • Pek, J. W., Anand, A., and Kai, T. (2012) Tudor domain proteins in development. Development 139, 2255-2266
    • (2012) Development , vol.139 , pp. 2255-2266
    • Pek, J.W.1    Anand, A.2    Kai, T.3
  • 19
    • 80053132089 scopus 로고    scopus 로고
    • Deciphering arginine methylation. Tudor tells the tale
    • Chen, C., Nott, T. J., Jin, J., and Pawson, T. (2011) Deciphering arginine methylation. Tudor tells the tale. Nat. Rev. Mol. Cell Biol. 12, 629-642
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 629-642
    • Chen, C.1    Nott, T.J.2    Jin, J.3    Pawson, T.4
  • 22
    • 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, M. V., Lee, J., Ward, I. M., Kim, J. E., Thompson, J. R., Chen, J., and Mer, G. (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    Chen, J.6    Mer, G.7
  • 23
    • 42649124614 scopus 로고    scopus 로고
    • Novel structural and functional mode of a knot essential for RNA binding activity of the Esa1 presumed chromodomain
    • Shimojo, H., Sano, N., Moriwaki, Y., Okuda, M., Horikoshi, M., and Nishimura, Y. (2008) Novel structural and functional mode of a knot essential for RNA binding activity of the Esa1 presumed chromodomain. J. Mol. Biol. 378, 987-1001
    • (2008) J. Mol. Biol. , vol.378 , pp. 987-1001
    • Shimojo, H.1    Sano, N.2    Moriwaki, Y.3    Okuda, M.4    Horikoshi, M.5    Nishimura, Y.6
  • 25
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang, Y., Fang, J., Bedford, M. T., Zhang, Y., and Xu, R. M. (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
  • 26
    • 0033794003 scopus 로고    scopus 로고
    • NMR spectroscopy. A multifaceted approach to macromolecular structure
    • Ferentz, A. E., and Wagner, G. (2000) NMR spectroscopy. A multifaceted approach to macromolecular structure. Q. Rev. Biophys. 33, 29-65
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 29-65
    • Ferentz, A.E.1    Wagner, G.2
  • 27
    • 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
  • 28
    • 34249765651 scopus 로고
    • NMRView. A computer program for visualization and analysis of NMR data
    • Johnson, B. A., and Blevins, R.A. (1994) NMRView. A computer program for visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 31
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Güntert, P., and Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319, 209-227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 33
    • 0035029325 scopus 로고    scopus 로고
    • SANE (Structure Assisted NOE Evaluation). An automated model-based approach for NOE assignment
    • Duggan, B. M., Legge, G. B., Dyson, H. J., and Wright, P. E. (2001) SANE (Structure Assisted NOE Evaluation). An automated model-based approach for NOE assignment. J. Biomol. NMR 19, 321-329
    • (2001) J. Biomol. NMR , vol.19 , pp. 321-329
    • Duggan, B.M.1    Legge, G.B.2    Dyson, H.J.3    Wright, P.E.4
  • 34
    • 0028393784 scopus 로고
    • The 13C chemical-shift index. A simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart, D. S., and Sykes, B. D. (1994) The 13C chemical-shift index. A simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR 4, 171-180
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 35
    • 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
  • 37
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR. Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR. Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    Macarthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 38
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL. A program for display and analysis of macromolecular structures
    • 29-32
    • Koradi, R., Billeter, M., and Wuthrich, K. (1996) MOLMOL. A program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55, 29-32
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 42
    • 77955391393 scopus 로고    scopus 로고
    • TheHADDOCKweb server for data-driven biomolecular docking
    • de Vries, S. J., van Dijk, M., and Bonvin, A. M. (2010) TheHADDOCKweb server for data-driven biomolecular docking. Nat. Protoc. 5, 883-897
    • (2010) Nat. Protoc. , vol.5 , pp. 883-897
    • De Vries, S.J.1    Van Dijk, M.2    Bonvin, A.M.3
  • 43
    • 67849110013 scopus 로고    scopus 로고
    • 3D-DART. A DNA structure modelling server
    • van Dijk, M., and Bonvin, A. M. (2009) 3D-DART. A DNA structure modelling server. Nucleic Acids Res. 37, W235-W239
    • (2009) Nucleic Acids Res. , vol.37
    • Van Dijk, M.1    Bonvin, A.M.2
  • 44
    • 36448949026 scopus 로고    scopus 로고
    • Multivalent engagement of chromatin modifications by linked binding modules
    • Ruthenburg, A. J., Li, H., Patel, D. J., and Allis, C. D. (2007) Multivalent engagement of chromatin modifications by linked binding modules. Nat. Rev. Mol. Cell Biol. 8, 983-994
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 983-994
    • Ruthenburg, A.J.1    Li, H.2    Patel, D.J.3    Allis, C.D.4
  • 45
    • 33644557129 scopus 로고    scopus 로고
    • RBP1 family proteins exhibit SUMOylation-dependent transcriptional repression and induce cell growth inhibition reminiscent of senescence
    • Binda, O., Roy, J. S., and Branton, P. E. (2006) RBP1 family proteins exhibit SUMOylation-dependent transcriptional repression and induce cell growth inhibition reminiscent of senescence. Mol. Cell Biol. 26, 1917-1931
    • (2006) Mol. Cell Biol. , vol.26 , pp. 1917-1931
    • Binda, O.1    Roy, J.S.2    Branton, P.E.3
  • 48
    • 84875278501 scopus 로고    scopus 로고
    • ARID4A and ARID4B regulate male fertility, a functional link to the AR and RB pathways
    • Wu, R. C., Jiang, M., Beaudet, A. L., and Wu, M. Y. (2013) ARID4A and ARID4B regulate male fertility, a functional link to the AR and RB pathways. Proc. Natl. Acad. Sci. U.S.A. 110, 4616-4621
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 4616-4621
    • Wu, R.C.1    Jiang, M.2    Beaudet, A.L.3    Wu, M.Y.4
  • 49
    • 84863664841 scopus 로고    scopus 로고
    • Allelic variation and differential expression of the mSIN3A histone deacetylase complex gene Arid4b promote mammary tumor growth and metastasis
    • Winter, S. F., Lukes, L., Walker, R. C., Welch, D. R., and Hunter, K. W. (2012) Allelic variation and differential expression of the mSIN3A histone deacetylase complex gene Arid4b promote mammary tumor growth and metastasis. PLoS Genet. 8, e1002735
    • (2012) PLoS Genet. , vol.8
    • Winter, S.F.1    Lukes, L.2    Walker, R.C.3    Welch, D.R.4    Hunter, K.W.5
  • 50
    • 77952698598 scopus 로고    scopus 로고
    • Retinoblastoma binding protein-1 (RBP1) is a Runx2 coactivator and promotes osteoblastic differentiation
    • Monroe, D. G., Hawse, J. R., Subramaniam, M., and Spelsberg, T. C. (2010) Retinoblastoma binding protein-1 (RBP1) is a Runx2 coactivator and promotes osteoblastic differentiation. BMC Musculoskelet. Disord. 11, 104
    • (2010) BMC Musculoskelet. Disord. , vol.11 , pp. 104
    • Monroe, D.G.1    Hawse, J.R.2    Subramaniam, M.3    Spelsberg, T.C.4
  • 53
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E., and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60, 2256-2268
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.