메뉴 건너뛰기




Volumn 414, Issue 2, 2011, Pages 165-176

Structure of the LSm657 complex: An assembly intermediate of the LSm1-7 and LSm2-8 rings

Author keywords

macromolecular complexes; mRNA degradation; mRNA splicing; NMR spectroscopy; TROSY

Indexed keywords

NUCLEIC ACID BINDING PROTEIN; PROTEIN LSM23; PROTEIN LSM5; PROTEIN LSM6; PROTEIN LSM657; PROTEIN LSM7; PROTEIN SM; PROTEIN SMD1; PROTEIN SMD2; PROTEIN SMD3; PROTEIN SME; PROTEIN SMF; PROTEIN SMG; UNCLASSIFIED DRUG;

EID: 81355148453     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.09.051     Document Type: Article
Times cited : (14)

References (39)
  • 2
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: Design principles of a dynamic RNP machine
    • Wahl M.C., Will C.L., and Luhrmann R. The spliceosome: design principles of a dynamic RNP machine Cell 136 2009 701 718
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Luhrmann, R.3
  • 3
    • 0035945611 scopus 로고    scopus 로고
    • Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle
    • DOI 10.1038/35054102
    • Stark H., Dube P., Luhrmann R., and Kastner B. Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle Nature 409 2001 539 542 (Pubitemid 32144362)
    • (2001) Nature , vol.409 , Issue.6819 , pp. 539-542
    • Stark, H.1    Dube, P.2    Luhrmann, R.3    Kastner, B.4
  • 4
    • 79957601559 scopus 로고    scopus 로고
    • Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis
    • Leung A.K., Nagai K., and Li J. Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis Nature 473 2011 536 539
    • (2011) Nature , vol.473 , pp. 536-539
    • Leung, A.K.1    Nagai, K.2    Li, J.3
  • 5
    • 0031841817 scopus 로고    scopus 로고
    • Capped mRNA degradation intermediates accumulate in the yeast spb8-2 mutant
    • Boeck R., Lapeyre B., Brown C.E., and Sachs A.B. Capped mRNA degradation intermediates accumulate in the yeast spb8-2 mutant Mol. Cell. Biol. 18 1998 5062 5072 (Pubitemid 28388089)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.9 , pp. 5062-5072
    • Boeck, R.1    Lapeyre, B.2    Brown, C.E.3    Sachs, A.B.4
  • 7
    • 0028997105 scopus 로고
    • Sm and Sm-like proteins belong to a large family: Identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs
    • Seraphin B. Sm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs EMBO J. 14 1995 2089 2098
    • (1995) EMBO J. , vol.14 , pp. 2089-2098
    • Seraphin, B.1
  • 8
    • 0029054377 scopus 로고
    • SnRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions
    • Hermann H., Fabrizio P., Raker V.A., Foulaki K., Hornig H., Brahms H., and Luhrmann R. snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions EMBO J. 14 1995 2076 2088
    • (1995) EMBO J. , vol.14 , pp. 2076-2088
    • Hermann, H.1    Fabrizio, P.2    Raker, V.A.3    Foulaki, K.4    Hornig, H.5    Brahms, H.6    Luhrmann, R.7
  • 9
    • 0029054375 scopus 로고
    • Identification and characterization of Uss1p (Sdb23p): A novel U6 snRNA-associated protein with significant similarity to core proteins of small nuclear ribonucleoproteins
    • Cooper M., Johnston L.H., and Beggs J.D. Identification and characterization of Uss1p (Sdb23p): a novel U6 snRNA-associated protein with significant similarity to core proteins of small nuclear ribonucleoproteins EMBO J. 14 1995 2066 2075
    • (1995) EMBO J. , vol.14 , pp. 2066-2075
    • Cooper, M.1    Johnston, L.H.2    Beggs, J.D.3
  • 10
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C., Higgins D.G., and Heringa J. T-Coffee: a novel method for fast and accurate multiple sequence alignment J. Mol. Biol. 302 2000 205 217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 11
    • 0033564627 scopus 로고    scopus 로고
    • Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin
    • DOI 10.1093/emboj/18.12.3451
    • Salgado-Garrido J., Bragado-Nilsson E., Kandels-Lewis S., and Seraphin B. Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin EMBO J. 18 1999 3451 3462 (Pubitemid 29276590)
    • (1999) EMBO Journal , vol.18 , Issue.12 , pp. 3451-3462
    • Salgado-Garrido, J.1    Bragado-Nilsson, E.2    Kandels-Lewis, S.3    Seraphin, B.4
  • 12
    • 78650273324 scopus 로고    scopus 로고
    • Functional organization of the Sm core in the crystal structure of human U1 snRNP
    • Weber G., Trowitzsch S., Kastner B., Luhrmann R., and Wahl M.C. Functional organization of the Sm core in the crystal structure of human U1 snRNP EMBO J. 29 2010 4172 4184
    • (2010) EMBO J. , vol.29 , pp. 4172-4184
    • Weber, G.1    Trowitzsch, S.2    Kastner, B.3    Luhrmann, R.4    Wahl, M.C.5
  • 13
    • 0035341325 scopus 로고    scopus 로고
    • RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex
    • DOI 10.1093/emboj/20.9.2293
    • Toro I., Thore S., Mayer C., Basquin J., Seraphin B., and Suck D. RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex EMBO J. 20 2001 2293 2303 (Pubitemid 32410598)
    • (2001) EMBO Journal , vol.20 , Issue.9 , pp. 2293-2303
    • Toro, I.1    Thore, S.2    Mayer, C.3    Basquin, J.4    Seraphin, B.5    Suck, D.6
  • 14
    • 0033569743 scopus 로고    scopus 로고
    • A doughnut-shaped heteromer of human Sm-like proteins binds to the 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro
    • DOI 10.1093/emboj/18.20.5789
    • Achsel T., Brahms H., Kastner B., Bachi A., Wilm M., and Luhrmann R. A doughnut-shaped heteromer of human Sm-like proteins binds to the 3′-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro EMBO J. 18 1999 5789 5802 (Pubitemid 29486396)
    • (1999) EMBO Journal , vol.18 , Issue.20 , pp. 5789-5802
    • Achsel, T.1    Brahms, H.2    Kastner, B.3    Bachi, A.4    Wilm, M.5    Luhrmann, R.6
  • 15
    • 18144402771 scopus 로고    scopus 로고
    • Reconstitution, of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function
    • DOI 10.1074/jbc.M414481200
    • Zaric B., Chami M., Remigy H., Engel A., Ballmer-Hofer K., Winkler F.K., and Kambach C. Reconstitution of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function J. Biol. Chem. 280 2005 16066 16075 (Pubitemid 40616731)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 16066-16075
    • Zaric, B.1    Chami, M.2    Remigy, H.3    Engel, A.4    Ballmer-Hofer, K.5    Winkler, F.K.6    Kambach, C.7
  • 16
    • 0033517098 scopus 로고    scopus 로고
    • Characterization of Sm-like proteins in yeast and their association with U6 snRNA
    • DOI 10.1093/emboj/18.15.4321
    • Mayes A.E., Verdone L., Legrain P., and Beggs J.D. Characterization of Sm-like proteins in yeast and their association with U6 snRNA EMBO J. 18 1999 4321 4331 (Pubitemid 29364134)
    • (1999) EMBO Journal , vol.18 , Issue.15 , pp. 4321-4331
    • Mayes, A.E.1    Verdone, L.2    Legrain, P.3    Beggs, J.D.4
  • 17
    • 0034732089 scopus 로고    scopus 로고
    • Yeast Sm-like proteins function in mRNA decapping and decay
    • DOI 10.1038/35006676
    • Tharun S., He W., Mayes A.E., Lennertz P., Beggs J.D., and Parker R. Yeast Sm-like proteins function in mRNA decapping and decay Nature 404 2000 515 518 (Pubitemid 30186896)
    • (2000) Nature , vol.404 , Issue.6777 , pp. 515-518
    • Tharun, S.1    He, W.2    Mayes, A.E.3    Lennertz, P.4    Beggs, J.D.5    Parker, R.6
  • 18
    • 34250804009 scopus 로고    scopus 로고
    • The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs
    • DOI 10.1261/rna.502507
    • Chowdhury A., Mukhopadhyay J., and Tharun S. The decapping activator LSm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs RNA 13 2007 998 1016 (Pubitemid 46984891)
    • (2007) RNA , vol.13 , Issue.7 , pp. 998-1016
    • Chowdhury, A.1    Mukhopadhyay, J.2    Tharun, S.3
  • 19
    • 70449727058 scopus 로고    scopus 로고
    • LSM1 over-expression in Saccharomyces cerevisiae depletes U6 snRNA levels
    • Luhtala N., and Parker R. LSM1 over-expression in Saccharomyces cerevisiae depletes U6 snRNA levels Nucleic Acids Res. 37 2009 5529 5536
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5529-5536
    • Luhtala, N.1    Parker, R.2
  • 20
    • 0033524941 scopus 로고    scopus 로고
    • Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs
    • DOI 10.1016/S0092-8674(00)80550-4
    • Kambach C., Walke S., Young R., Avis J.M., de la Fortelle E., and Raker V.A. Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs Cell 96 1999 375 387 (Pubitemid 29077591)
    • (1999) Cell , vol.96 , Issue.3 , pp. 375-387
    • Kambach, C.1    Walke, S.2    Young, R.3    Avis, J.M.4    De La Fortelle, E.5    Raker, V.A.6    Luhrmann, R.7    Li, J.8    Nagai, K.9
  • 21
    • 0036290884 scopus 로고    scopus 로고
    • Archaeal Sm proteins form heptameric and hexameric complexes: Crystal structures of the Sm1 and Sm2 proteins from the hyperthermophile Archaeoglobus fulgidus
    • DOI 10.1016/S0022-2836(02)00406-0
    • Toro I., Basquin J., Teo-Dreher H., and Suck D. Archaeal Sm proteins form heptameric and hexameric complexes: crystal structures of the Sm1 and Sm2 proteins from the hyperthermophile Archaeoglobus fulgidus J. Mol. Biol. 320 2002 129 142 (Pubitemid 34722238)
    • (2002) Journal of Molecular Biology , vol.320 , Issue.1 , pp. 129-142
    • Toro, I.1    Basquin, J.2    Teo-Dreher, H.3    Suck, D.4
  • 22
    • 40849094144 scopus 로고    scopus 로고
    • Crystal structure of LSm3 octamer from Saccharomyces cerevisiae: Implications for LSm ring organisation and recruitment
    • Naidoo N., Harrop S.J., Sobti M., Haynes P.A., Szymczyna B.R., and Williamson J.R. Crystal structure of LSm3 octamer from Saccharomyces cerevisiae: implications for LSm ring organisation and recruitment J. Mol. Biol. 377 2008 1357 1371
    • (2008) J. Mol. Biol. , vol.377 , pp. 1357-1371
    • Naidoo, N.1    Harrop, S.J.2    Sobti, M.3    Haynes, P.A.4    Szymczyna, B.R.5    Williamson, J.R.6
  • 23
    • 54549102220 scopus 로고    scopus 로고
    • An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs
    • Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., and Englbrecht C. An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs Cell 135 2008 497 509
    • (2008) Cell , vol.135 , pp. 497-509
    • Chari, A.1    Golas, M.M.2    Klingenhager, M.3    Neuenkirchen, N.4    Sander, B.5    Englbrecht, C.6
  • 31
    • 0031575412 scopus 로고    scopus 로고
    • Electron microscopy of assembly intermediates of the snRNP core: Morphological similarities between the RNA-free (E.F.G) protein heteromer and the intact snRNP core
    • DOI 10.1006/jmbi.1996.0713
    • Plessel G., Luhrmann R., and Kastner B. Electron microscopy of assembly intermediates of the snRNP core: morphological similarities between the RNA-free (E.F.G.) protein heteromer and the intact snRNP core J. Mol. Biol. 265 1997 87 94 (Pubitemid 27110646)
    • (1997) Journal of Molecular Biology , vol.265 , Issue.2 , pp. 87-94
    • Plessel, G.1    Luhrmann, R.2    Kastner, B.3
  • 32
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • 51-5
    • Koradi, R., Billeter, M. & Wuthrich, K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-5, 29-32.
    • (1996) J. Mol. Graphics , vol.14 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 33
    • 0242380623 scopus 로고    scopus 로고
    • Sm-like proteins in Eubacteria: The crystal structure of the Hfq protein from Escherichia coli
    • DOI 10.1093/nar/gkg480
    • Sauter C., Basquin J., and Suck D. Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli Nucleic Acids Res. 31 2003 4091 4098 (Pubitemid 37448496)
    • (2003) Nucleic Acids Research , vol.31 , Issue.14 , pp. 4091-4098
    • Sauter, C.1    Basquin, J.2    Suck, D.3
  • 34
    • 63649099704 scopus 로고    scopus 로고
    • Crystal structure of human spliceosomal U1 snRNP at 5.5 Å resolution
    • Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., and Nagai K. Crystal structure of human spliceosomal U1 snRNP at 5.5 Å resolution Nature 458 2009 475 480
    • (2009) Nature , vol.458 , pp. 475-480
    • Pomeranz Krummel, D.A.1    Oubridge, C.2    Leung, A.K.3    Li, J.4    Nagai, K.5
  • 35
    • 0141924550 scopus 로고    scopus 로고
    • The Prp19p-associated complex in spliceosome activation
    • Chan S.P., Kao D.I., Tsai W.Y., and Cheng S.C. The Prp19p-associated complex in spliceosome activation Science 302 2003 279 282
    • (2003) Science , vol.302 , pp. 279-282
    • Chan, S.P.1    Kao, D.I.2    Tsai, W.Y.3    Cheng, S.C.4
  • 36
    • 0030612833 scopus 로고    scopus 로고
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution Proc. Natl Acad. Sci. USA 94 1997 12366 12371
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 39
    • 0030007060 scopus 로고    scopus 로고
    • The snRNP core assembly pathway: Identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro
    • Raker V.A., Plessel G., and Luhrmann R. The snRNP core assembly pathway: identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro EMBO J. 15 1996 2256 2269
    • (1996) EMBO J. , vol.15 , pp. 2256-2269
    • Raker, V.A.1    Plessel, G.2    Luhrmann, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.