메뉴 건너뛰기




Volumn 34, Issue 1, 2006, Pages 305-312

Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; INTRINSICALLY DISORDERED PROTEIN; PROTEIN; SERINE; UNCLASSIFIED DRUG;

EID: 31544433157     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkj424     Document Type: Article
Times cited : (87)

References (59)
  • 1
    • 0026716104 scopus 로고
    • SR proteins: A conserved family of pre-mRNA splicing factors
    • Zahler,A.M., Lane,W.S., Stolk,J.A. and Roth,M.B. (1992) SR proteins: A conserved family of pre-mRNA splicing factors. Genes Dev., 6, 837-847.
    • (1992) Genes Dev. , vol.6 , pp. 837-847
    • Zahler, A.M.1    Lane, W.S.2    Stolk, J.A.3    Roth, M.B.4
  • 2
    • 0027137934 scopus 로고
    • Specific interactions between proteins implicated in splice site selection and regulated alternative splicing
    • Wu,J.Y. and Maniatis,T. (1993) Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell, 75, 1061-1070.
    • (1993) Cell , vol.75 , pp. 1061-1070
    • Wu, J.Y.1    Maniatis, T.2
  • 3
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley,B.R. (2000) Sorting out the complexity of SR protein functions. RNA, 6, 1197-1211.
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 4
    • 14644445227 scopus 로고    scopus 로고
    • SRprises along a messenger's journey
    • Huang,Y. and Steitz,J.A. (2005) SRprises along a messenger's journey. Mol. Cell, 17, 613-615.
    • (2005) Mol. Cell , vol.17 , pp. 613-615
    • Huang, Y.1    Steitz, J.A.2
  • 5
    • 14644431487 scopus 로고    scopus 로고
    • Broad specificity of SR (serine/arginine) proteins in the regulation of alternative splicing of pre-messenger RNA
    • Bourgeois,C.F.,Lejeune,F. and Stevenin,J. (2004) Broad specificity of SR (serine/arginine) proteins in the regulation of alternative splicing of pre-messenger RNA. Prog. Nucleic Acid Res. Mol. Biol., 78, 37-88.
    • (2004) Prog. Nucleic Acid Res. Mol. Biol. , vol.78 , pp. 37-88
    • Bourgeois, C.F.1    Lejeune, F.2    Stevenin, J.3
  • 6
    • 0029372979 scopus 로고
    • The superfamily of arginine/serine-rich splicing factors
    • Fu,X.D. (1995) The superfamily of arginine/serine-rich splicing factors. RNA, 1, 663-680.
    • (1995) RNA , vol.1 , pp. 663-680
    • Fu, X.D.1
  • 9
    • 0035823011 scopus 로고    scopus 로고
    • A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer
    • Kielkopf,C.L., Rodionova,N.A., Green,M.R. and Burley,S.K. (2001) A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer. Cell, 106, 595-605.
    • (2001) Cell , vol.106 , pp. 595-605
    • Kielkopf, C.L.1    Rodionova, N.A.2    Green, M.R.3    Burley, S.K.4
  • 10
    • 1242316952 scopus 로고    scopus 로고
    • Arginine-serine-rich domains bound at splicing enhancers contact the branchpoint to promote prespliceosome assembly
    • Shen,H., Kan,J.L. and Green,M.R. (2004) Arginine-serine-rich domains bound at splicing enhancers contact the branchpoint to promote prespliceosome assembly. Mol. Cell, 13, 367-376.
    • (2004) Mol. Cell , vol.13 , pp. 367-376
    • Shen, H.1    Kan, J.L.2    Green, M.R.3
  • 11
    • 0032038213 scopus 로고    scopus 로고
    • Arginine/serine-rich domains of SR proteins can function as activators of pre-mRNA splicing
    • Graveley,B.R.and Maniatis,T.(1998) Arginine/serine-rich domains of SR proteins can function as activators of pre-mRNA splicing. Mol. Cell, 1, 765-771.
    • (1998) Mol. Cell , vol.1 , pp. 765-771
    • Graveley, B.R.1    Maniatis, T.2
  • 12
    • 0031929940 scopus 로고    scopus 로고
    • A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm
    • Caceres,J.F., Screaton,G.R. and Krainer,A.R. (1998) A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm. Genes Dev., 12, 55-66.
    • (1998) Genes Dev. , vol.12 , pp. 55-66
    • Caceres, J.F.1    Screaton, G.R.2    Krainer, A.R.3
  • 14
    • 8844219677 scopus 로고    scopus 로고
    • Involvement of SR proteins in mRNA surveillance
    • Zhang,Z. and Krainer,A.R. (2004) Involvement of SR proteins in mRNA surveillance. Mol. Cell, 16, 597-607.
    • (2004) Mol. Cell , vol.16 , pp. 597-607
    • Zhang, Z.1    Krainer, A.R.2
  • 15
    • 0032737702 scopus 로고    scopus 로고
    • SR protein kinases: The splice of life
    • Stojdl,D.F. and Bell,J.C. (1999) SR protein kinases: The splice of life. Biochem. Cell Biol., 77, 293-298.
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 293-298
    • Stojdl, D.F.1    Bell, J.C.2
  • 16
    • 0345801103 scopus 로고    scopus 로고
    • Phosphorylation-dependent control of the pre-mRNA splicing machinery
    • Soret,J. and Tazi,J. (2003) Phosphorylation-dependent control of the pre-mRNA splicing machinery. Prog. Mol. Subcell. Biol., 31, 89-126.
    • (2003) Prog. Mol. Subcell. Biol. , vol.31 , pp. 89-126
    • Soret, J.1    Tazi, J.2
  • 17
    • 26944489645 scopus 로고    scopus 로고
    • Building specificity with nonspecific RNA-binding proteins
    • Singh,R. and Valcarcel,J. (2005) Building specificity with nonspecific RNA-binding proteins. Nature Struct. Mol. Biol., 12, 645-653.
    • (2005) Nature Struct. Mol. Biol. , vol.12 , pp. 645-653
    • Singh, R.1    Valcarcel, J.2
  • 18
    • 0032526604 scopus 로고    scopus 로고
    • Interaction between the N-terminal domain of human DNA topoisomerase I and the arginine-serine domain of its substrate determines phosphorylation of SF2/ASF splicing factor
    • Labourier,E., Rossi,F., Gallouzi,I.E., Allemand,E., Divita,G. and Tazi,J. (1998) Interaction between the N-terminal domain of human DNA topoisomerase I and the arginine-serine domain of its substrate determines phosphorylation of SF2/ASF splicing factor. Nucleic Acids Res., 26, 2955-2962.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2955-2962
    • Labourier, E.1    Rossi, F.2    Gallouzi, I.E.3    Allemand, E.4    Divita, G.5    Tazi, J.6
  • 19
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright,P.E. and Dyson,H.J. (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol., 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 20
    • 0034669882 scopus 로고    scopus 로고
    • Why are 'natively unfolded' proteins unstructured under physiologic conditions?
    • Uversky,V.N., Gillespie,J.R. and Fink,A.L. (2000) Why are 'natively unfolded' proteins unstructured under physiologic conditions? Proteins, 41, 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 24
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson,H.J. and Wright,P.E. (2005) Intrinsically unstructured proteins and their functions. Nature Rev. Mol. Cell. Biol., 6, 197-208.
    • (2005) Nature Rev. Mol. Cell. Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 25
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa,P. (2005) The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett., 579, 3346-3354.
    • (2005) FEBS Lett. , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 27
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker,A.K., Cortese,M.S., Romero,P., Iakoucheva,L.M. and Uversky,V.N. (2005) Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J., 272, 5129-5148.
    • (2005) FEBS J. , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 30
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm,U. and Sander,C. (1994) Enlarged representative set of protein structures. Protein Sci., 3, 522-524.
    • (1994) Protein Sci. , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 35
    • 17844399803 scopus 로고    scopus 로고
    • Addressing the intrinsic disorder bottleneck in structural proteomics
    • Oldfield,C.J., Ulrich,E.L., Cheng,Y., Dunker,A.K. and Markley,J.L. (2005) Addressing the intrinsic disorder bottleneck in structural proteomics. Proteins, 59, 444-453.
    • (2005) Proteins , vol.59 , pp. 444-453
    • Oldfield, C.J.1    Ulrich, E.L.2    Cheng, Y.3    Dunker, A.K.4    Markley, J.L.5
  • 36
    • 84856043672 scopus 로고
    • The mathematical theory of communication
    • 379-423 and
    • Shannon,C.E. (1948) The mathematical theory of communication. Bell Syst. Tech. J., 27, 379-423 and 623-656.
    • (1948) Bell Syst. Tech. J. , vol.27 , pp. 623-656
    • Shannon, C.E.1
  • 37
    • 0001514262 scopus 로고
    • Statistic of local complexity in amino acid sequences and sequence databases
    • Wootton,J.C. (1993) Statistic of local complexity in amino acid sequences and sequence databases. Comput. Chem., 17, 149-163.
    • (1993) Comput. Chem. , vol.17 , pp. 149-163
    • Wootton, J.C.1
  • 39
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte,J. and Doolittle,R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 40
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky,V.N. (2002) What does it mean to be natively unfolded? Eur. J. Biochem., 269, 2-12.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 41
    • 0028361031 scopus 로고
    • Accuracy of protein flexibility predictions
    • Vihinen,M., Torkkila,E. and Riikonen,P. (1994) Accuracy of protein flexibility predictions. Proteins, 19, 141-149.
    • (1994) Proteins , vol.19 , pp. 141-149
    • Vihinen, M.1    Torkkila, E.2    Riikonen, P.3
  • 42
    • 0033957834 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
    • Bairoch,A. and Apweiler,R. (2000) The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucleic Acids Res., 28, 45-48.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 43
    • 0042819915 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins evolve by repeat expansion
    • Tompa,P. (2003) Intrinsically unstructured proteins evolve by repeat expansion. Bioessays, 25, 847-855.
    • (2003) Bioessays , vol.25 , pp. 847-855
    • Tompa, P.1
  • 44
    • 0031860374 scopus 로고    scopus 로고
    • RNA recognition by RNP proteins during RNA processing
    • Varani,G. and Nagai,K. (1998) RNA recognition by RNP proteins during RNA processing. Annu. Rev. Biophys Biomol. Struct., 27, 407-445.
    • (1998) Annu. Rev. Biophys Biomol. Struct. , vol.27 , pp. 407-445
    • Varani, G.1    Nagai, K.2
  • 45
    • 0032483346 scopus 로고    scopus 로고
    • Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains
    • Konrat,R., Krautler,B., Weiskirchen,R. and Bister,K. (1998) Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains. J. Biol. Chem., 273, 23233-23240.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23233-23240
    • Konrat, R.1    Krautler, B.2    Weiskirchen, R.3    Bister, K.4
  • 47
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson,H.J. and Wright,P.E. (2002) Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol., 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 48
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa,P., Szasz,C. and Buday,L. (2005) Structural disorder throws new light on moonlighting. Trends Biochem. Sci., 30, 484-489.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3
  • 49
    • 0345099646 scopus 로고    scopus 로고
    • Arginine/serine repeats are sufficient to constitute a splicing activation domain
    • Philipps,D., Celotto,A.M., Wang,Q.Q., Tarng,R.S. and Graveley,B.R. (2003) Arginine/serine repeats are sufficient to constitute a splicing activation domain. Nucleic Acids Res., 31, 6502-6508.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6502-6508
    • Philipps, D.1    Celotto, A.M.2    Wang, Q.Q.3    Tarng, R.S.4    Graveley, B.R.5
  • 50
    • 0035964258 scopus 로고    scopus 로고
    • Transportin-SR2 mediates nuclear import of phosphorylated SR proteins
    • Lai,M.C., Lin,R.I. and Tarn,W.Y. (2001) Transportin-SR2 mediates nuclear import of phosphorylated SR proteins. Proc. Natl Acad. Sci. USA, 98, 10154-10159.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10154-10159
    • Lai, M.C.1    Lin, R.I.2    Tarn, W.Y.3
  • 51
    • 0033564196 scopus 로고    scopus 로고
    • Developmental regulation of SR protein phosphorylation and activity
    • Sanford,J.R. and Bruzik,J.P. (1999) Developmental regulation of SR protein phosphorylation and activity. Genes Dev., 13, 1513-1518.
    • (1999) Genes Dev. , vol.13 , pp. 1513-1518
    • Sanford, J.R.1    Bruzik, J.P.2
  • 53
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong,S.E., Mittler,G. and Mann,M. (2004) Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nature Methods, 1, 119-126.
    • (2004) Nature Methods , vol.1 , pp. 119-126
    • Ong, S.E.1    Mittler, G.2    Mann, M.3
  • 54
    • 0035131438 scopus 로고    scopus 로고
    • Roles of partly unfolded conformations in macromolecular self-assembly
    • Namba,K. (2001) Roles of partly unfolded conformations in macromolecular self-assembly. Genes Cells, 6, 1-12.
    • (2001) Genes Cells , vol.6 , pp. 1-12
    • Namba, K.1
  • 55
    • 0004039245 scopus 로고
    • Absorption and Circular Dichroism Spectra of Individual Proteins from Escherichia coli Ribosomes
    • Biological Research Center, Institute of Protein Research, Pushchino, USSR
    • Venyaminov,S., Gudkov,A., Gogia,Z. and Tumanova,L. (1981) Absorption and Circular Dichroism Spectra of Individual Proteins from Escherichia coli Ribosomes. Biological Research Center, Institute of Protein Research, Pushchino, USSR.
    • (1981)
    • Venyaminov, S.1    Gudkov, A.2    Gogia, Z.3    Tumanova, L.4
  • 56
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • Ban,N., Nissen,P., Hansen,J., Moore,P.B. and Steitz,T.A. (2000) The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science, 289, 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 57
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded
    • Denning,D.P., Patel,S.S., Uversky,V., Fink,A.L. and Rexach,M. (2003) Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded. Proc. Natl Acad. Sci. USA, 100, 2450-2455.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Uversky, V.3    Fink, A.L.4    Rexach, M.5
  • 58
    • 0042671357 scopus 로고    scopus 로고
    • Pre-mRNA splicing: Awash in a sea of proteins
    • Jurica,M.S. and Moore,M.J. (2003) Pre-mRNA splicing: Awash in a sea of proteins. Mol. Cell, 12, 5-14.
    • (2003) Mol. Cell , vol.12 , pp. 5-14
    • Jurica, M.S.1    Moore, M.J.2
  • 59
    • 0029377886 scopus 로고
    • SR proteins escort the U4/U6.U5 tri-snRNP to the spliceosome
    • Roscigno,R.F. and Garcia-Blanco,M.A. (1995) SR proteins escort the U4/ U6.U5 tri-snRNP to the spliceosome. RNA, 1, 692-706.
    • (1995) RNA , vol.1 , pp. 692-706
    • Roscigno, R.F.1    Garcia-Blanco, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.