메뉴 건너뛰기




Volumn 393, Issue 2, 2009, Pages 409-424

Structural Studies of FF Domains of the Transcription Factor CA150 Provide Insights into the Organization of FF Domain Tandem Arrays

Author keywords

diffusion tensor; dynamics; ModelFree; phosphopeptide; relaxation

Indexed keywords

LEUCINE ZIPPER PROTEIN; RNA POLYMERASE II; TRANSCRIPTION ELONGATION FACTOR; TRANSCRIPTION FACTOR; PEPTIDE; TCERG1 PROTEIN, HUMAN; TRANSACTIVATOR PROTEIN;

EID: 70349416397     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.08.049     Document Type: Article
Times cited : (8)

References (44)
  • 1
    • 1842287996 scopus 로고    scopus 로고
    • CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription
    • Sune C., Hayashi T., Liu Y., Lane W.S., Young R.A., and Garcia-Blanco M.A. CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription. Mol. Cell. Biol. 17 (1997) 6029-6039
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6029-6039
    • Sune, C.1    Hayashi, T.2    Liu, Y.3    Lane, W.S.4    Young, R.A.5    Garcia-Blanco, M.A.6
  • 2
    • 0345161783 scopus 로고    scopus 로고
    • Transcriptional cofactor CA150 regulates RNA polymerase II elongation in a TATA-box-dependent manner
    • Sune C., and Garcia-Blanco M.A. Transcriptional cofactor CA150 regulates RNA polymerase II elongation in a TATA-box-dependent manner. Mol. Cell. Biol. 19 (1999) 4719-4728
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4719-4728
    • Sune, C.1    Garcia-Blanco, M.A.2
  • 3
    • 0030027483 scopus 로고    scopus 로고
    • Identification of Prp40, a novel essential yeast splicing factor associated with the U1 small nuclear ribonucleoprotein particle
    • Kao H.-Y., and Siliciano P.G. Identification of Prp40, a novel essential yeast splicing factor associated with the U1 small nuclear ribonucleoprotein particle. Mol. Cell. Biol. 16 (1996) 960-967
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 960-967
    • Kao, H.-Y.1    Siliciano, P.G.2
  • 4
    • 0033168375 scopus 로고    scopus 로고
    • The FF domain: a novel motif that often accompanies WW domains
    • Bedford M.T., and Leder P. The FF domain: a novel motif that often accompanies WW domains. Trends Biochem. Sci. 24 (1999) 264-265
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 264-265
    • Bedford, M.T.1    Leder, P.2
  • 5
    • 4744355045 scopus 로고    scopus 로고
    • The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo
    • Lin K.-T., Lu R.-M., and Tarn W.-Y. The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo. Mol. Cell. Biol. 24 (2004) 9176-9185
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9176-9185
    • Lin, K.-T.1    Lu, R.-M.2    Tarn, W.-Y.3
  • 6
    • 11344265267 scopus 로고    scopus 로고
    • An FF domain-dependent protein interaction mediates a signalling pathway for growth factor-induced gene expression
    • Jiang W., Sordella R., Chen G.C., Hakre S., Roy A.L., and Settleman J. An FF domain-dependent protein interaction mediates a signalling pathway for growth factor-induced gene expression. Mol. Cell 17 (2005) 23-35
    • (2005) Mol. Cell , vol.17 , pp. 23-35
    • Jiang, W.1    Sordella, R.2    Chen, G.C.3    Hakre, S.4    Roy, A.L.5    Settleman, J.6
  • 7
    • 6344277922 scopus 로고    scopus 로고
    • FF domains of CA150 bind transcription and splicing factors through multiple weak interactions
    • Smith M.J., Kulkarni S., and Pawson T. FF domains of CA150 bind transcription and splicing factors through multiple weak interactions. Mol. Cell. Biol. 24 (2004) 9274-9285
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9274-9285
    • Smith, M.J.1    Kulkarni, S.2    Pawson, T.3
  • 8
    • 0034255028 scopus 로고    scopus 로고
    • Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II
    • Carty S.M., Goldstrohm A.C., Sune C., Garcia-Blanco M.A., and Greenleaf A.L. Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II. Proc. Natl Acad. Sci. USA 97 (2000) 9015-9020
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9015-9020
    • Carty, S.M.1    Goldstrohm, A.C.2    Sune, C.3    Garcia-Blanco, M.A.4    Greenleaf, A.L.5
  • 9
    • 0034704145 scopus 로고    scopus 로고
    • The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • Morris D.P., and Greenleaf A.L. The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem. 275 (2000) 39935-39943
    • (2000) J. Biol. Chem. , vol.275 , pp. 39935-39943
    • Morris, D.P.1    Greenleaf, A.L.2
  • 10
    • 0031711073 scopus 로고    scopus 로고
    • Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex
    • Neubauer G., King A., Rappsilber J., Calvio C., Watson M., and Ajuh P. Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex. Nature Genet. 20 (1998) 46-50
    • (1998) Nature Genet. , vol.20 , pp. 46-50
    • Neubauer, G.1    King, A.2    Rappsilber, J.3    Calvio, C.4    Watson, M.5    Ajuh, P.6
  • 11
    • 0034774728 scopus 로고    scopus 로고
    • The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1
    • Goldstrohm A.C., Albrecht T.R., Sune C., Bedford M.T., and Garcia-Blanco M.A. The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1. Mol. Cell. Biol. 21 (2001) 7617-7628
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7617-7628
    • Goldstrohm, A.C.1    Albrecht, T.R.2    Sune, C.3    Bedford, M.T.4    Garcia-Blanco, M.A.5
  • 12
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • Zhou Z., Licklider L.J., Gygi S.P., and Reed R. Comprehensive proteomic analysis of the human spliceosome. Nature 419 (2002) 182-185
    • (2002) Nature , vol.419 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4
  • 13
    • 0036407694 scopus 로고    scopus 로고
    • The structure of an FF domain from human HYPA/FBP11
    • Allen M., Friedler A., Schon O., and Bycroft M. The structure of an FF domain from human HYPA/FBP11. J. Mol. Biol. 323 (2002) 411-416
    • (2002) J. Mol. Biol. , vol.323 , pp. 411-416
    • Allen, M.1    Friedler, A.2    Schon, O.3    Bycroft, M.4
  • 14
    • 10844238946 scopus 로고    scopus 로고
    • Expanding the functional repertoire of CTD Kinase I and RNA Polymerase II: Novel phosphoCTD-associating proteins in the yeast proteome
    • Phatnani H.P., Jones J.C., and Greenleaf A.L. Expanding the functional repertoire of CTD Kinase I and RNA Polymerase II: Novel phosphoCTD-associating proteins in the yeast proteome. Biochemistry 43 (2004) 15702-15719
    • (2004) Biochemistry , vol.43 , pp. 15702-15719
    • Phatnani, H.P.1    Jones, J.C.2    Greenleaf, A.L.3
  • 15
    • 0009370184 scopus 로고
    • A unique structure at the carboxyl terminus of the largest subunit of the eukaryotic RNA polymerase II
    • Corden J.L., Cadena D.L., Ahearn J.M., and Dahmus M.E. A unique structure at the carboxyl terminus of the largest subunit of the eukaryotic RNA polymerase II. Proc. Natl Acad. Sci. USA 82 (1985) 7934-7938
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 7934-7938
    • Corden, J.L.1    Cadena, D.L.2    Ahearn, J.M.3    Dahmus, M.E.4
  • 16
    • 0024815284 scopus 로고
    • An enlarged largest subunit of Plasmodium falciparum RNA polymerase II defines conserved and variable RNA polymerase domains
    • Li W.-B., Bzik B., Gu H., Tanaka M., Fox B.A., and Inselburg J. An enlarged largest subunit of Plasmodium falciparum RNA polymerase II defines conserved and variable RNA polymerase domains. Nucleic Acids Res. 17 (1989) 9621-9636
    • (1989) Nucleic Acids Res. , vol.17 , pp. 9621-9636
    • Li, W.-B.1    Bzik, B.2    Gu, H.3    Tanaka, M.4    Fox, B.A.5    Inselburg, J.6
  • 17
    • 0025915378 scopus 로고
    • Identification of phosphorylation sites in the repetitive carboxyl-terminal domain of the mouse RNA polymerase II largest subunit
    • Zhang J., and Corden J.L. Identification of phosphorylation sites in the repetitive carboxyl-terminal domain of the mouse RNA polymerase II largest subunit. J. Biol. Chem. 266 (1991) 2290-2296
    • (1991) J. Biol. Chem. , vol.266 , pp. 2290-2296
    • Zhang, J.1    Corden, J.L.2
  • 18
    • 33644863653 scopus 로고    scopus 로고
    • The structure of Prp40 FF1 domain and its interaction with the crn-TPR1 motif of Clf1 gives a new insight into the binding mode of FF domains
    • Gasch A., Wiesner S., Martin-Malpartida P., Ramirez-Espain X., Ruiz L., and Macias M.J. The structure of Prp40 FF1 domain and its interaction with the crn-TPR1 motif of Clf1 gives a new insight into the binding mode of FF domains. J. Biol. Chem. 281 (2006) 356-364
    • (2006) J. Biol. Chem. , vol.281 , pp. 356-364
    • Gasch, A.1    Wiesner, S.2    Martin-Malpartida, P.3    Ramirez-Espain, X.4    Ruiz, L.5    Macias, M.J.6
  • 19
    • 58149288620 scopus 로고    scopus 로고
    • Solution structure of the yeast URN1 splicing factor FF domain: Comparative analysis of charge distributions in FF domain structures - FFs and SURPs, two domains with a similar fold
    • Bonet R., Ramirez-Espain X., and Macias M.J. Solution structure of the yeast URN1 splicing factor FF domain: Comparative analysis of charge distributions in FF domain structures - FFs and SURPs, two domains with a similar fold. Proteins: Struct. Funct. Genet. 73 (2008) 1001-1009
    • (2008) Proteins: Struct. Funct. Genet. , vol.73 , pp. 1001-1009
    • Bonet, R.1    Ramirez-Espain, X.2    Macias, M.J.3
  • 20
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 29-32
    • (1996) J. Mol. Graph. , vol.14 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 21
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease
    • Kay L.E., Torchia D.A., and Bax A. Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28 (1989) 8972-8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 22
    • 84945737762 scopus 로고
    • A leisurely look at the bootstrap, the jackknife, and cross-validation
    • Efron B., and Gong G. A leisurely look at the bootstrap, the jackknife, and cross-validation. Am. Stat. 37 (1983) 36-48
    • (1983) Am. Stat. , vol.37 , pp. 36-48
    • Efron, B.1    Gong, G.2
  • 23
    • 70349432165 scopus 로고    scopus 로고
    • Crystal structure of the three tandem FF domains of the transcription elongation regulator CA150
    • Lu M., Yang J., Ren Z., Sabui S., Espejo A., Bedford M.T., et al. Crystal structure of the three tandem FF domains of the transcription elongation regulator CA150. J. Mol. Biol. 393 (2009) 397-408
    • (2009) J. Mol. Biol. , vol.393 , pp. 397-408
    • Lu, M.1    Yang, J.2    Ren, Z.3    Sabui, S.4    Espejo, A.5    Bedford, M.T.6
  • 26
    • 0032877215 scopus 로고    scopus 로고
    • Yeast ortholog of the Drosophila crooked neck protein promotes spliceosome assembly through stable U4/U6.U5 snRNP addition
    • Chung S., McLean M.R., and Rymond B.C. Yeast ortholog of the Drosophila crooked neck protein promotes spliceosome assembly through stable U4/U6.U5 snRNP addition. RNA 5 (1999) 1042-1054
    • (1999) RNA , vol.5 , pp. 1042-1054
    • Chung, S.1    McLean, M.R.2    Rymond, B.C.3
  • 27
    • 58149306033 scopus 로고    scopus 로고
    • The FF domains of yeast U1 snURP protein Prp40 mediate interactions with Luc7 and Snu71
    • Ester C., and Uetz P. The FF domains of yeast U1 snURP protein Prp40 mediate interactions with Luc7 and Snu71. BMC Biochem. 9 (2008) 29
    • (2008) BMC Biochem. , vol.9 , pp. 29
    • Ester, C.1    Uetz, P.2
  • 28
    • 33745473130 scopus 로고    scopus 로고
    • Human transcription elongation factor CA150 localizes to splicing factor-rich nuclear speckles and assembles transcription and splicing components into complexes through its amino and carboxy regions
    • Sanchez-Alvarez M., Goldstrohm A.C., Garcia-Blanco M., and Sune C. Human transcription elongation factor CA150 localizes to splicing factor-rich nuclear speckles and assembles transcription and splicing components into complexes through its amino and carboxy regions. Mol. Cell. Biol. 26 (2006) 4998-5014
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 4998-5014
    • Sanchez-Alvarez, M.1    Goldstrohm, A.C.2    Garcia-Blanco, M.3    Sune, C.4
  • 29
    • 33750621978 scopus 로고    scopus 로고
    • Gender biased differential alternative splicing patterns of the transcriptional cofactor CA150 gene in Schistosoma mansoni
    • DeMarco R., Oliveira K.C., Venancio T.M., and Verjovski-Almeida S. Gender biased differential alternative splicing patterns of the transcriptional cofactor CA150 gene in Schistosoma mansoni. Mol. Biochem. Parasitol. 150 (2006) 123-131
    • (2006) Mol. Biochem. Parasitol. , vol.150 , pp. 123-131
    • DeMarco, R.1    Oliveira, K.C.2    Venancio, T.M.3    Verjovski-Almeida, S.4
  • 30
    • 0036928101 scopus 로고    scopus 로고
    • Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40
    • Wiesner S., Stier G., Sattler M., and Macias M.J. Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40. J. Mol. Biol. 324 (2002) 807-822
    • (2002) J. Mol. Biol. , vol.324 , pp. 807-822
    • Wiesner, S.1    Stier, G.2    Sattler, M.3    Macias, M.J.4
  • 32
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C., Xia T.-H., Billeter M., Güntert P., and Wüthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 6 (1995) 1-10
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 33
    • 0029437296 scopus 로고
    • Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution
    • Kay L.E. Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution. Prog. Biophys. Mol. Biol. 63 (1995) 277-299
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 277-299
    • Kay, L.E.1
  • 34
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M., Schleucher J., and Griesinger C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. NMR Spectrosc. 34 (1999) 93-158
    • (1999) Prog. NMR Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 35
    • 0028282555 scopus 로고
    • Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation
    • Farrow N.A., Muhandiram R., Singer A.U., Pascal S.M., Kay C.M., and Gish G. Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry 33 (1994) 5984-6003
    • (1994) Biochemistry , vol.33 , pp. 5984-6003
    • Farrow, N.A.1    Muhandiram, R.2    Singer, A.U.3    Pascal, S.M.4    Kay, C.M.5    Gish, G.6
  • 36
    • 0037063506 scopus 로고    scopus 로고
    • An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates
    • Korzhnev D.M., Skrynnikov N.R., Millet O., Torchia D., and Kay L.E. An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates. J. Am. Chem. Soc. 124 (2002) 10743-10753
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10743-10753
    • Korzhnev, D.M.1    Skrynnikov, N.R.2    Millet, O.3    Torchia, D.4    Kay, L.E.5
  • 38
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 39
    • 0028545648 scopus 로고
    • α J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
    • α J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J. Biomol. NMR 4 (1994) 871-878
    • (1994) J. Biomol. NMR , vol.4 , pp. 871-878
    • Kubinowa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 41
    • 0031110495 scopus 로고    scopus 로고
    • Floating stereospecific assignment revisited: application to an 18 kDa protein and comparison with J-coupling data
    • Folmer R.H., Hilbers C.W., Konings R.N., and Nilges M. Floating stereospecific assignment revisited: application to an 18 kDa protein and comparison with J-coupling data. J. Biomol. NMR 9 (1997) 245-258
    • (1997) J. Biomol. NMR , vol.9 , pp. 245-258
    • Folmer, R.H.1    Hilbers, C.W.2    Konings, R.N.3    Nilges, M.4
  • 42
    • 0347988396 scopus 로고    scopus 로고
    • Ambiguous NOEs and automated NOE assignment
    • Nilges M., and O'Donoghue S.I. Ambiguous NOEs and automated NOE assignment. Prog. NMR Spectrosc. 32 (1998) 107-139
    • (1998) Prog. NMR Spectrosc. , vol.32 , pp. 107-139
    • Nilges, M.1    O'Donoghue, S.I.2
  • 43
    • 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., Kapstein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kapstein, R.4    Thornton, J.M.5
  • 44
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme
    • Mandel A.M., Akke M., and Palmer III A.G. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol. 246 (1995) 144-163
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer III, A.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.