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Volumn 448, Issue , 2008, Pages 57-74

Chapter 4 Reconstitution of Recombinant Human LSm Complexes for Biochemical, Biophysical, and Cell Biological Studies

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN LSM; RECOMBINANT PROTEIN; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 57749186710     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)02604-9     Document Type: Review
Times cited : (6)

References (39)
  • 1
    • 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
    • Achsel T., Brahms H., Kastner B., Bachi A., Wilm M., and Lührmann 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
    • (1999) EMBO J. , vol.18 , pp. 5789-5802
    • Achsel, T.1    Brahms, H.2    Kastner, B.3    Bachi, A.4    Wilm, M.5    Lührmann, R.6
  • 2
    • 3042684849 scopus 로고    scopus 로고
    • Novel Sm-like proteins with long C-terminal tails and associated methyltransferases
    • Albrecht M., and Lengauer T. Novel Sm-like proteins with long C-terminal tails and associated methyltransferases. FEBS Lett. 569 (2004) 18-26
    • (2004) FEBS Lett. , vol.569 , pp. 18-26
    • Albrecht, M.1    Lengauer, T.2
  • 3
    • 9144267469 scopus 로고    scopus 로고
    • Novel conserved domains in proteins with predicted roles in eukaryotic cell-cycle regulation, decapping and RNA stability
    • Anantharaman V., and Aravind L. Novel conserved domains in proteins with predicted roles in eukaryotic cell-cycle regulation, decapping and RNA stability. BMC. Genomics 5 (2004) 45
    • (2004) BMC. Genomics , vol.5 , pp. 45
    • Anantharaman, V.1    Aravind, L.2
  • 4
    • 18344396487 scopus 로고    scopus 로고
    • LSm proteins and RNA processing
    • Beggs J.D. LSm proteins and RNA processing. Biochem. Soc. Trans. 33 (2005) 433-438
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 433-438
    • Beggs, J.D.1
  • 5
    • 11144340226 scopus 로고    scopus 로고
    • Baculovirus expression system for heterologous multiprotein complexes
    • Berger I., Fitzgerald D.J., and Richmond T.J. Baculovirus expression system for heterologous multiprotein complexes. Nat. Biotechnol. 22 (2004) 1583-1587
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1583-1587
    • Berger, I.1    Fitzgerald, D.J.2    Richmond, T.J.3
  • 7
    • 0033776919 scopus 로고    scopus 로고
    • Functional characterization of nuclear localization signals in yeast Sm proteins
    • Bordonne R. Functional characterization of nuclear localization signals in yeast Sm proteins. Mol. Cell Biol. 20 (2000) 7943-7954
    • (2000) Mol. Cell Biol. , vol.20 , pp. 7943-7954
    • Bordonne, R.1
  • 8
    • 0034599976 scopus 로고    scopus 로고
    • A Sm-like protein complex that participates in mRNA degradation
    • Bouveret E., Rigaut G., Shevchenko A., Wilm M., and Séraphin B. A Sm-like protein complex that participates in mRNA degradation. EMBO J. 19 (2000) 1661-1671
    • (2000) EMBO J. , vol.19 , pp. 1661-1671
    • Bouveret, E.1    Rigaut, G.2    Shevchenko, A.3    Wilm, M.4    Séraphin, B.5
  • 9
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein
    • Brahms H., Meheus L., de V B., Fischer U., and Lührmann R. Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA 7 (2001) 1531-1542
    • (2001) RNA , vol.7 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    de V, B.3    Fischer, U.4    Lührmann, R.5
  • 10
    • 0035895435 scopus 로고    scopus 로고
    • Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli
    • Fribourg S., Romier C., Werten S., Gangloff Y.G., Poterszman A., and Moras D. Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli. J. Mol. Biol. 306 (2001) 363-373
    • (2001) J. Mol. Biol. , vol.306 , pp. 363-373
    • Fribourg, S.1    Romier, C.2    Werten, S.3    Gangloff, Y.G.4    Poterszman, A.5    Moras, D.6
  • 12
    • 0030963019 scopus 로고    scopus 로고
    • Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens
    • Fromont-Racine M., Rain J.C., and Legrain P. Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nat. Genet. 16 (1997) 277-282
    • (1997) Nat. Genet. , vol.16 , pp. 277-282
    • Fromont-Racine, M.1    Rain, J.C.2    Legrain, P.3
  • 13
    • 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 Lührmann 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    Lührmann, R.7
  • 14
    • 0036909093 scopus 로고    scopus 로고
    • The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
    • Ingelfinger D., Arndt-Jovin D.J., Lührmann R., and Achsel T. The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA 8 (2002) 1489-1501
    • (2002) RNA , vol.8 , pp. 1489-1501
    • Ingelfinger, D.1    Arndt-Jovin, D.J.2    Lührmann, R.3    Achsel, T.4
  • 15
    • 0033117879 scopus 로고    scopus 로고
    • Structure and assembly of the spliceosomal small nuclear ribonucleoprotein particles
    • Kambach C., Walke S., and Nagai K. Structure and assembly of the spliceosomal small nuclear ribonucleoprotein particles. Curr. Opin. Struct. Biol. 9 (1999) 222-230
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 222-230
    • Kambach, C.1    Walke, S.2    Nagai, K.3
  • 16
    • 0033524941 scopus 로고    scopus 로고
    • Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs
    • Kambach C., Walke S., Young R., Avis J.M., de la F.E., Raker V.A., Lührmann R., Li J., and Nagai K. Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Cell 96 (1999) 375-387
    • (1999) Cell , vol.96 , pp. 375-387
    • Kambach, C.1    Walke, S.2    Young, R.3    Avis, J.M.4    de la, F.E.5    Raker, V.A.6    Lührmann, R.7    Li, J.8    Nagai, K.9
  • 17
    • 23944455046 scopus 로고    scopus 로고
    • LSm proteins form heptameric rings that bind to RNA via repeating motifs
    • Khusial P., Plaag R., and Zieve G.W. LSm proteins form heptameric rings that bind to RNA via repeating motifs. Trends Biochem. Sci. 30 (2005) 522-528
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 522-528
    • Khusial, P.1    Plaag, R.2    Zieve, G.W.3
  • 18
    • 2442676387 scopus 로고    scopus 로고
    • Two-promoter vector is highly efficient for overproduction of protein complexes
    • Kim K.J., Kim H.E., Lee K.H., Han W., Yi M.J., Jeong J., and Oh B.H. Two-promoter vector is highly efficient for overproduction of protein complexes. Protein Sci. 13 (2004) 1698-1703
    • (2004) Protein Sci. , vol.13 , pp. 1698-1703
    • Kim, K.J.1    Kim, H.E.2    Lee, K.H.3    Han, W.4    Yi, M.J.5    Jeong, J.6    Oh, B.H.7
  • 19
    • 20444382808 scopus 로고    scopus 로고
    • The Gemin6-Gemin7 heterodimer from the survival of motor neurons complex has an Sm protein-like structure
    • Ma Y., Dostie J., Dreyfuss G., and Van Duyne G.D. The Gemin6-Gemin7 heterodimer from the survival of motor neurons complex has an Sm protein-like structure. Structure 13 (2005) 883-892
    • (2005) Structure , vol.13 , pp. 883-892
    • Ma, Y.1    Dostie, J.2    Dreyfuss, G.3    Van Duyne, G.D.4
  • 20
    • 0036809734 scopus 로고    scopus 로고
    • SMN-mediated assembly of RNPs: A complex story
    • Meister G., Eggert C., and Fischer U. SMN-mediated assembly of RNPs: A complex story. Trends Cell Biol. 12 (2002) 472-478
    • (2002) Trends Cell Biol. , vol.12 , pp. 472-478
    • Meister, G.1    Eggert, C.2    Fischer, U.3
  • 22
    • 0037378351 scopus 로고    scopus 로고
    • The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs)
    • Mura C., Kozhukhovsky A., Gingery M., Phillips M., and Eisenberg D. The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs). Protein Sci. 12 (2003) 832-847
    • (2003) Protein Sci. , vol.12 , pp. 832-847
    • Mura, C.1    Kozhukhovsky, A.2    Gingery, M.3    Phillips, M.4    Eisenberg, D.5
  • 23
    • 0035022015 scopus 로고    scopus 로고
    • Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein
    • Pannone B.K., Kim S.D., Noe D.A., and Wolin S.L. Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein. Genetics 158 (2001) 187-196
    • (2001) Genetics , vol.158 , pp. 187-196
    • Pannone, B.K.1    Kim, S.D.2    Noe, D.A.3    Wolin, S.L.4
  • 24
    • 0141818102 scopus 로고    scopus 로고
    • Unique Sm core structure of U7 snRNPs: Assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing
    • Pillai R.S., Grimmler M., Meister G., Will C.L., Lührmann R., Fischer U., and Schumperli D. Unique Sm core structure of U7 snRNPs: Assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing. Genes Dev. 17 (2003) 2321-2333
    • (2003) Genes Dev. , vol.17 , pp. 2321-2333
    • Pillai, R.S.1    Grimmler, M.2    Meister, G.3    Will, C.L.4    Lührmann, R.5    Fischer, U.6    Schumperli, D.7
  • 25
    • 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
    • Plessel G., Lührmann 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
    • (1997) J. Mol. Biol. , vol.265 , pp. 87-94
    • Plessel, G.1    Lührmann, R.2    Kastner, B.3
  • 26
    • 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 Lührmann 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    Lührmann, R.3
  • 27
    • 0033564627 scopus 로고    scopus 로고
    • Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin
    • Salgado-Garrido J., Bragado-Nilsson E., Kandels-Lewis S., and Séraphin B. Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin. EMBO J. 18 (1999) 3451-3462
    • (1999) EMBO J. , vol.18 , pp. 3451-3462
    • Salgado-Garrido, J.1    Bragado-Nilsson, E.2    Kandels-Lewis, S.3    Séraphin, B.4
  • 28
    • 0025351553 scopus 로고
    • Enhanced translational efficiency with two-cistron expression system
    • Schoner B.E., Belagaje R.M., and Schoner R.G. Enhanced translational efficiency with two-cistron expression system. Methods Enzymol. 185 (1990) 94-103
    • (1990) Methods Enzymol. , vol.185 , pp. 94-103
    • Schoner, B.E.1    Belagaje, R.M.2    Schoner, R.G.3
  • 29
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein
    • Schumacher M.A., Pearson R.F., Moller T., Valentin-Hansen P., and Brennan R.G. Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein. EMBO J. 21 (2002) 3546-3556
    • (2002) EMBO J. , vol.21 , pp. 3546-3556
    • Schumacher, M.A.1    Pearson, R.F.2    Moller, T.3    Valentin-Hansen, P.4    Brennan, R.G.5
  • 30
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • Sheth U., and Parker R. Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300 (2003) 805-808
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 31
    • 33847360037 scopus 로고    scopus 로고
    • The Lsm2-8 complex determines nuclear localization of the spliceosomal U6 snRNA
    • Spiller M.P., Boon K.L., Reijns M.A., and Beggs J.D. The Lsm2-8 complex determines nuclear localization of the spliceosomal U6 snRNA. Nucleic Acids Res. 35 (2007) 923-929
    • (2007) Nucleic Acids Res. , vol.35 , pp. 923-929
    • Spiller, M.P.1    Boon, K.L.2    Reijns, M.A.3    Beggs, J.D.4
  • 32
    • 57749206336 scopus 로고    scopus 로고
    • University of Cambridge, UK Ph.D. thesis
    • Walke S. (2000), University of Cambridge, UK Ph.D. thesis
    • (2000)
    • Walke, S.1
  • 33
    • 0026919628 scopus 로고
    • In vitro reconstitution of U1 and U2 snRNPs from isolated proteins and snRNA
    • Sumpter V., Kahrs A., Fischer U., Kornstadt U., and Lührmann R. In vitro reconstitution of U1 and U2 snRNPs from isolated proteins and snRNA. Mol. Biol. Rep. 16 (1992) 229-240
    • (1992) Mol. Biol. Rep. , vol.16 , pp. 229-240
    • Sumpter, V.1    Kahrs, A.2    Fischer, U.3    Kornstadt, U.4    Lührmann, R.5
  • 34
  • 35
    • 0035930337 scopus 로고    scopus 로고
    • Targeting an mRNA for decapping: Displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs
    • Tharun S., and Parker R. Targeting an mRNA for decapping: Displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Mol. Cell 8 (2001) 1075-1083
    • (2001) Mol. Cell , vol.8 , pp. 1075-1083
    • Tharun, S.1    Parker, R.2
  • 36
    • 0035863194 scopus 로고    scopus 로고
    • Sm protein-Sm site RNA interactions within the inner ring of the spliceosomal snRNP core structure
    • Urlaub H., Raker V.A., Kostka S., and Lührmann R. Sm protein-Sm site RNA interactions within the inner ring of the spliceosomal snRNP core structure. EMBO J. 20 (2001) 187-196
    • (2001) EMBO J. , vol.20 , pp. 187-196
    • Urlaub, H.1    Raker, V.A.2    Kostka, S.3    Lührmann, R.4
  • 37
    • 33749324465 scopus 로고    scopus 로고
    • Sm core variation in spliceosomal small nuclear ribonucleoproteins from Trypanosoma brucei
    • Wang P., Palfi Z., Preusser C., Lucke S., Lane W.S., Kambach C., and Bindereif A. Sm core variation in spliceosomal small nuclear ribonucleoproteins from Trypanosoma brucei. EMBO J. 25 (2006) 4513-4523
    • (2006) EMBO J. , vol.25 , pp. 4513-4523
    • Wang, P.1    Palfi, Z.2    Preusser, C.3    Lucke, S.4    Lane, W.S.5    Kambach, C.6    Bindereif, A.7
  • 38
    • 2142819496 scopus 로고    scopus 로고
    • Why do cells need an assembly machine for RNA-protein complexes
    • Yong J., Wan L., and Dreyfuss G. Why do cells need an assembly machine for RNA-protein complexes. Trends Cell Biol. 14 (2004) 226-232
    • (2004) Trends Cell Biol. , vol.14 , pp. 226-232
    • Yong, J.1    Wan, L.2    Dreyfuss, G.3
  • 39
    • 18144402771 scopus 로고    scopus 로고
    • Reconstitution of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function
    • 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
    • (2005) J. Biol. Chem. , vol.280 , 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


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