메뉴 건너뛰기




Volumn 73, Issue 4, 2008, Pages 1001-1009

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

Author keywords

FF domains; NMR structures; URN1 protein; Yeast

Indexed keywords

FUNGAL PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; URN1 PROTEIN; CARRIER PROTEIN; NUCLEAR PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; URN1 PROTEIN, S CEREVISIAE;

EID: 58149288620     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22127     Document Type: Article
Times cited : (21)

References (33)
  • 1
    • 0033168375 scopus 로고    scopus 로고
    • The FF domain: A novel motif that often accompanies WW domains
    • DOI 10.1016/S0968-0004(99)01417-6, PII S0968000499014176
    • Bedford MT, Leder P. The FF domain: a novel motif that often accompanies WW domains. Trends Biochem Sci 1999;24:264-265. (Pubitemid 29301689)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.7 , pp. 264-265
    • Bedford, M.T.1    Leder, P.2
  • 2
    • 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
    • DOI 10.1074/jbc.M508047200
    • Gasch A, Wiesner S, Martin-Malpartida P, Ramirez-Espain X, Ruiz L, Macias MJ. 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 2006;281:356-364. (Pubitemid 43671196)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.1 , pp. 356-364
    • Gasch, A.1    Wiesner, S.2    Martin-Malpartida, P.3    Ramirez-Espain, X.4    Ruiz, L.5    Macias, M.J.6
  • 3
    • 0036407694 scopus 로고    scopus 로고
    • The structure of an FF domain from human HYPA/FBP11
    • Allen M, Friedler A, Schon O, Bycroft M. The structure of an FF domain from human HYPA/FBP11. J Mol Biol 2002;323:411-416.
    • (2002) J Mol Biol , vol.323 , pp. 411-416
    • Allen, M.1    Friedler, A.2    Schon, O.3    Bycroft, M.4
  • 4
    • 7744221200 scopus 로고    scopus 로고
    • Conspicuous accumulation of transcription elongation repressor hrp130/CA150 on the intron-rich Balbiani ring 3 gene
    • DOI 10.1007/s00412-004-0314-4
    • Sun X, Zhao J, Kylberg K, Soop T, Palka K, Sonnhammer E, Visa N, Alzhanova-Ericsson AT, Daneholt B. Conspicuous accumulation of transcription elongation repressor hrp130/CA150 on the intronrich Balbiani ring 3 gene. Chromosoma 2004;113:244-257. (Pubitemid 39462367)
    • (2004) Chromosoma , vol.113 , Issue.5 , pp. 244-257
    • Sun, X.1    Zhao, J.2    Kylberg, K.3    Soop, T.4    Palka, K.5    Sonnhammer, E.6    Visa, N.7    Alzhanova-Ericsson, A.T.8    Daneholt, B.9
  • 5
    • 33746363486 scopus 로고    scopus 로고
    • Domains, motifs, and scaffolds: The role of modular interactions in the evolution and wiring of cell signaling circuits
    • DOI 10.1146/annurev.biochem.75.103004.142710
    • Bhattacharyya RP, Remenyi A, Yeh BJ, Lim WA. Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. Annu Rev Biochem 2006;75:655-680. (Pubitemid 44118047)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 655-680
    • Bhattacharyya, R.P.1    Remenyi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 7
    • 11344265267 scopus 로고    scopus 로고
    • An FF domain-dependent protein interaction mediates a signaling pathway for growth factor-induced gene expression
    • DOI 10.1016/j.molcel.2004.11.024, PII S1097276504007154
    • Jiang W, Sordella R, Chen GC, Hakre S, Roy AL, Settleman J. An FF domain-dependent protein interaction mediates a signaling pathway for growth factor-induced gene expression. Mol Cell 2005; 17:23-35. (Pubitemid 40075362)
    • (2005) Molecular Cell , vol.17 , Issue.1 , pp. 23-35
    • Jiang, W.1    Sordella, R.2    Chen, G.-C.3    Hakre, S.4    Roy, A.L.5    Settleman, J.6
  • 8
    • 6344277922 scopus 로고    scopus 로고
    • FF domains of CA150 bind transcription and splicing factors through multiple weak interactions
    • DOI 10.1128/MCB.24.21.9274-9285.2004
    • Smith MJ, Kulkarni S, Pawson T. FF domains of CA150 bind transcription and splicing factors through multiple weak interactions. Mol Cell Biol 2004;24:9274-9285. (Pubitemid 39391666)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.21 , pp. 9274-9285
    • Smith, M.J.1    Kulkarni, S.2    Pawson, T.3
  • 9
    • 0032877215 scopus 로고    scopus 로고
    • Yeast ortholog of the Drosophila crooked neck protein promotes spliceosome assembly through stable U4/U6.U5 snRNP addition
    • DOI 10.1017/S1355838299990635
    • Chung S, McLean MR, Rymond BC. Yeast ortholog of the Drosophila crooked neck protein promotes spliceosome assembly through stable U4/U6.U5 snRNP addition. RNA 1999;5:1042-1054. (Pubitemid 29365334)
    • (1999) RNA , vol.5 , Issue.8 , pp. 1042-1054
    • Chung, S.1    McLean, M.R.2    Rymond, B.C.3
  • 10
    • 0042208446 scopus 로고    scopus 로고
    • Genetic interactions with CLF1 identify additional pre-mRNA splicing factors and a link between activators of yeast vesicular transport and splicing
    • Vincent K, Wang Q, Jay S, Hobbs K, Rymond BC. Genetic interactions with CLF1 identify additional pre-mRNA splicing factors and a link between activators of yeast vesicular transport and splicing. Genetics 2003;164:895-907. (Pubitemid 36935668)
    • (2003) Genetics , vol.164 , Issue.3 , pp. 895-907
    • Vincent, K.1    Wang, Q.2    Jay, S.3    Hobbs, K.4    Rymond, B.C.5
  • 11
    • 0037424381 scopus 로고    scopus 로고
    • The Clf1p splicing factor promotes spliceosome assembly through N-terminal tetratricopeptide repeat contacts
    • DOI 10.1074/jbc.M210839200
    • Wang Q, Hobbs K, Lynn B, Rymond BC. The Clf1p splicing factor promotes spliceosome assembly through N-terminal tetratricopeptide repeat contacts. J Biol Chem 2003;278:7875-7883. (Pubitemid 36800522)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 7875-7883
    • Wang, Q.1    Hobbs, K.2    Lynn, B.3    Rymond, B.C.4
  • 13
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995;247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 14
    • 0028341660 scopus 로고
    • Conservation of regulated alternative splicing and identification of functional domains in vertebrate homologs to the Drosophila splicing regulator, suppressor-of-white-apricot
    • Denhez F, Lafyatis R. Conservation of regulated alternative splicing and identification of functional domains in vertebrate homologs to the Drosophila splicing regulator, suppressor-of-white-apricot. J Biol Chem 1994;269:16170-16179. (Pubitemid 24209308)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.23 , pp. 16170-16179
    • Denhez, F.1    Lafyatis, R.2
  • 15
    • 0027943711 scopus 로고
    • SWAP pre-mRNA splicing regulators are a novel, ancient protein family sharing a highly conserved sequence motif with the prp21 family of constitutive splicing proteins
    • Spikes DA, Kramer J, Bingham PM, Van Doren K. SWAP premRNA splicing regulators are a novel, ancient protein family sharing a highly conserved sequence motif with the prp21 family of constitutive splicing proteins. Nucleic Acids Res 1994;22:4510-4519. (Pubitemid 24336425)
    • (1994) Nucleic Acids Research , vol.22 , Issue.21 , pp. 4510-4519
    • Spikes, D.A.1    Kramer, J.2    Bingham, P.M.3    Van Doren, K.4
  • 16
    • 33846216009 scopus 로고    scopus 로고
    • Solution Structures of the SURP Domains and the Subunit-Assembly Mechanism within the Splicing Factor SF3a Complex in 17S U2 snRNP
    • DOI 10.1016/j.str.2006.09.009, PII S0969212606003959
    • Kuwasako K, He F, Inoue M, Tanaka A, Sugano S, Guntert P, Muto Y, Yokoyama S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP. Structure 2006;14:1677-1689. (Pubitemid 46107275)
    • (2006) Structure , vol.14 , Issue.11 , pp. 1677-1689
    • Kuwasako, K.1    He, F.2    Inoue, M.3    Tanaka, A.4    Sugano, S.5    Guntert, P.6    Muto, Y.7    Yokoyama, S.8
  • 17
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • DOI 10.1023/A:1011254402785
    • Marley J, Lu M, Bracken C. A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 2001;20:71-75. (Pubitemid 32519656)
    • (2001) Journal of Biomolecular NMR , vol.20 , Issue.1 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 19
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C, Xia T-H, Billeter M, Güntert P, Wüthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J Biomol NMR 1995;5:1-10.
    • (1995) J Biomol NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 21
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from b-spectrin
    • DOI 10.1006/jmbi.1997.1044
    • Nilges M, Macias MJ, O'Donoghue SI, Oschkinat H. Automated NOESY Interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin Homology domain from b-spectrin. J Mol Biol 1997;269:408-422. (Pubitemid 27267762)
    • (1997) Journal of Molecular Biology , vol.269 , Issue.3 , pp. 408-422
    • Nilges, M.1    MacIas, M.J.2    O'Donoghue, S.I.3    Oschkinat, H.4
  • 22
    • 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, Wüthrich K. MOLMOL: a program for display and analysis macromolecular structures. J Mol Graphics 1996;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
  • 25
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • DOI 10.1093/nar/25.24.4876
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997;24:4876-4882. (Pubitemid 28022245)
    • (1997) Nucleic Acids Research , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 27
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov IN, Bourne PE. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng 1998;11:739-747. (Pubitemid 28434482)
    • (1998) Protein Engineering , vol.11 , Issue.9 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 30
    • 0028785252 scopus 로고
    • Does Vav bind to F-actin through a CH domain?
    • Castresana J, Saraste M. Does Vav bind to F-actin through a CH domain? FEBS Lett 1995;374:149-151.
    • (1995) FEBS Lett , vol.374 , pp. 149-151
    • Castresana, J.1    Saraste, M.2
  • 31
    • 11444265046 scopus 로고    scopus 로고
    • Structure and dynamics of the human pleckstrin DEP Domain: Distinct molecular features of a novel DEP domain subfamily
    • DOI 10.1002/prot.20320
    • Civera C, Simon B, Stier G, Sattler M, Macias MJ. Structure and dynamics of the human pleckstrin DEP domain: distinct molecular features of a novel DEP domain subfamily. Proteins 2005;58:354-366. (Pubitemid 40081121)
    • (2005) Proteins: Structure, Function and Genetics , vol.58 , Issue.2 , pp. 354-366
    • Civera, C.1    Simon, B.2    Stier, G.3    Sattler, M.4    Macias, M.J.5
  • 33
    • 0028244489 scopus 로고
    • Structure of the pleckstrin homology domain from b-spectrin
    • DOI 10.1038/369675a0
    • Macias MJ, Musacchio A, Ponstingl H, Nilges M, Saraste M, Oschkinat H. Structure of the pleckstrin homology domain from bspectrin. Nature 1994;369:675-677. (Pubitemid 24199475)
    • (1994) Nature , vol.369 , Issue.6482 , pp. 675-677
    • Macias, M.J.1    Musacchio, A.2    Ponstingl, H.3    Nilges, M.4    Saraste, M.5    Oschkinat, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.