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Volumn 368, Issue 3, 2007, Pages 677-690

Distant Segments of Saccharomyces cerevisiae scR1 RNA Promote Assembly and Function of the Signal Recognition Particle

Author keywords

mutagenesis; ribonucleoprotein; RNA structure; signal recognition particle; SRP

Indexed keywords

ELONGATION FACTOR; FUNGAL PROTEIN; PROTEIN SCR1; RIBONUCLEOPROTEIN; RNA; SIGNAL RECOGNITION PARTICLE; UNCLASSIFIED DRUG;

EID: 34047130640     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.02.056     Document Type: Article
Times cited : (5)

References (43)
  • 1
    • 18844387083 scopus 로고    scopus 로고
    • Signal recognition particles in chloroplasts, bacteria, yeast and mammals
    • Pool M.R. Signal recognition particles in chloroplasts, bacteria, yeast and mammals. Mol. Membr. Biol. 22 (2005) 3-15
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 3-15
    • Pool, M.R.1
  • 2
    • 17044419154 scopus 로고    scopus 로고
    • Targeting proteins to membranes: structure of the signal recognition particle
    • Egea P.F., Stroud R.M., and Walter P. Targeting proteins to membranes: structure of the signal recognition particle. Curr. Opin. Struct. Biol. 15 (2005) 213-220
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 213-220
    • Egea, P.F.1    Stroud, R.M.2    Walter, P.3
  • 3
    • 13844266603 scopus 로고    scopus 로고
    • The signal recognition particle and its interactions during protein targeting
    • Halic M., and Beckmann R. The signal recognition particle and its interactions during protein targeting. Curr. Opin. Struct. Biol. 15 (2005) 116-125
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 116-125
    • Halic, M.1    Beckmann, R.2
  • 4
    • 0004489150 scopus 로고
    • Structure of the signal recognition particle by electron microscopy
    • Andrews D.W., Walter P., and Ottensmeyer F.P. Structure of the signal recognition particle by electron microscopy. Proc. Natl Acad. Sci. USA 82 (1985) 785-789
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 785-789
    • Andrews, D.W.1    Walter, P.2    Ottensmeyer, F.P.3
  • 5
    • 0023443260 scopus 로고
    • Evidence for an extended 7SL RNA structure in the signal recognition particle
    • Andrews D.W., Walter P., and Ottensmeyer F.P. Evidence for an extended 7SL RNA structure in the signal recognition particle. EMBO J. 6 (1987) 3471-3477
    • (1987) EMBO J. , vol.6 , pp. 3471-3477
    • Andrews, D.W.1    Walter, P.2    Ottensmeyer, F.P.3
  • 6
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic M., Becker T., Pool M.R., Spahn C.M., Grassucci R.A., Frank J., and Beckmann R. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427 (2004) 808-814
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 7
    • 0024817509 scopus 로고
    • Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate
    • Wolin S.L., and Walter P. Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate. J. Cell Biol. 109 (1989) 2617-2622
    • (1989) J. Cell Biol. , vol.109 , pp. 2617-2622
    • Wolin, S.L.1    Walter, P.2
  • 8
    • 0034254190 scopus 로고    scopus 로고
    • Elongation arrest is a physiologically important function of signal recognition particle
    • Mason N., Ciufo L.F., and Brown J.D. Elongation arrest is a physiologically important function of signal recognition particle. EMBO J. 19 (2000) 4164-4174
    • (2000) EMBO J. , vol.19 , pp. 4164-4174
    • Mason, N.1    Ciufo, L.F.2    Brown, J.D.3
  • 9
    • 27644589630 scopus 로고    scopus 로고
    • The Trypanosoma brucei signal recognition particle lacks the Alu-domain-binding proteins: purification and functional analysis of its binding proteins by RNAi
    • Lustig Y., Goldshmidt H., Uliel S., and Michaeli S. The Trypanosoma brucei signal recognition particle lacks the Alu-domain-binding proteins: purification and functional analysis of its binding proteins by RNAi. J. Cell Sci. 118 (2005) 4551-4562
    • (2005) J. Cell Sci. , vol.118 , pp. 4551-4562
    • Lustig, Y.1    Goldshmidt, H.2    Uliel, S.3    Michaeli, S.4
  • 11
    • 0025601549 scopus 로고
    • The methionine-rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence
    • Zopf D., Bernstein H.D., Johnson A.E., and Walter P. The methionine-rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. EMBO J. 9 (1990) 4511-4517
    • (1990) EMBO J. , vol.9 , pp. 4511-4517
    • Zopf, D.1    Bernstein, H.D.2    Johnson, A.E.3    Walter, P.4
  • 12
    • 0026533588 scopus 로고
    • The methionine-rich domain of the 54 kDa subunit of signal recognition particle is sufficient for the interaction with signal sequences
    • Lütcke H., High S., Römisch K., Ashford A., and Dobberstein B. The methionine-rich domain of the 54 kDa subunit of signal recognition particle is sufficient for the interaction with signal sequences. EMBO J. 11 (1992) 1543-1551
    • (1992) EMBO J. , vol.11 , pp. 1543-1551
    • Lütcke, H.1    High, S.2    Römisch, K.3    Ashford, A.4    Dobberstein, B.5
  • 13
    • 0024121564 scopus 로고
    • Binding sites of the 19-kDa and 68/72-kDa signal recognition particle (SRP) proteins on SRP RNA as determined by protein-RNA "footprinting"
    • Siegel V., and Walter P. Binding sites of the 19-kDa and 68/72-kDa signal recognition particle (SRP) proteins on SRP RNA as determined by protein-RNA "footprinting". Proc. Natl Acad. Sci. USA 85 (1988) 1801-1805
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 1801-1805
    • Siegel, V.1    Walter, P.2
  • 14
    • 0027322152 scopus 로고
    • Assembly of the 68- and 72-kD proteins of the signal recognition particle with 7S RNA
    • Lütcke H., Prehn S., Ashford A.J., Remus M., Frank R., and Dobberstein B. Assembly of the 68- and 72-kD proteins of the signal recognition particle with 7S RNA. J. Cell Biol. 121 (1993) 977-985
    • (1993) J. Cell Biol. , vol.121 , pp. 977-985
    • Lütcke, H.1    Prehn, S.2    Ashford, A.J.3    Remus, M.4    Frank, R.5    Dobberstein, B.6
  • 15
    • 0034626729 scopus 로고    scopus 로고
    • Structure and assembly of the Alu domain of the mammalian signal recognition particle
    • Weichenrieder O., Wild K., Strub K., and Cusack S. Structure and assembly of the Alu domain of the mammalian signal recognition particle. Nature 408 (2000) 167-173
    • (2000) Nature , vol.408 , pp. 167-173
    • Weichenrieder, O.1    Wild, K.2    Strub, K.3    Cusack, S.4
  • 16
    • 0035051603 scopus 로고    scopus 로고
    • Hierarchical assembly of the Alu domain of the mammalian signal recognition particle
    • Weichenrieder O., Stehlin C., Kapp U., Birse D.E., Timmins P.A., Strub K., and Cusack S. Hierarchical assembly of the Alu domain of the mammalian signal recognition particle. RNA 7 (2001) 731-740
    • (2001) RNA , vol.7 , pp. 731-740
    • Weichenrieder, O.1    Stehlin, C.2    Kapp, U.3    Birse, D.E.4    Timmins, P.A.5    Strub, K.6    Cusack, S.7
  • 17
    • 0030785575 scopus 로고    scopus 로고
    • A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle
    • Thomas Y., Bui N., and Strub K. A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle. Nucl. Acids Res. 25 (1997) 1920-1929
    • (1997) Nucl. Acids Res. , vol.25 , pp. 1920-1929
    • Thomas, Y.1    Bui, N.2    Strub, K.3
  • 18
    • 0346096862 scopus 로고    scopus 로고
    • Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognition
    • Terzi L., Pool M.R., Dobberstein B., and Strub K. Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognition. Biochemistry 43 (2004) 107-117
    • (2004) Biochemistry , vol.43 , pp. 107-117
    • Terzi, L.1    Pool, M.R.2    Dobberstein, B.3    Strub, K.4
  • 19
    • 0032859702 scopus 로고    scopus 로고
    • The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure
    • Strub K., Fornallaz M., and Bui N. The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure. RNA 5 (1999) 1333-1347
    • (1999) RNA , vol.5 , pp. 1333-1347
    • Strub, K.1    Fornallaz, M.2    Bui, N.3
  • 20
    • 0346992205 scopus 로고    scopus 로고
    • Saccharomyces SRP RNA secondary structures: a conserved S-domain and extended Alu-domain
    • Van Nues R.W., and Brown J.D. Saccharomyces SRP RNA secondary structures: a conserved S-domain and extended Alu-domain. RNA 10 (2004) 75-89
    • (2004) RNA , vol.10 , pp. 75-89
    • Van Nues, R.W.1    Brown, J.D.2
  • 21
    • 2442651537 scopus 로고    scopus 로고
    • Identification and comparative analysis of components from the signal recognition particle in protozoa and fungi
    • doi:10.1186/1471-2164-5-5
    • Rosenblad M.A., Zwieb C., and Samuelsson T. Identification and comparative analysis of components from the signal recognition particle in protozoa and fungi. BMC Genomics 5 (2004) 5 doi:10.1186/1471-2164-5-5
    • (2004) BMC Genomics , vol.5 , pp. 5
    • Rosenblad, M.A.1    Zwieb, C.2    Samuelsson, T.3
  • 22
    • 0036682153 scopus 로고    scopus 로고
    • Prediction of signal recognition particle RNA genes
    • Regalia M., Rosenblad M.A., and Samuelsson T. Prediction of signal recognition particle RNA genes. Nucl. Acids Res. 30 (2002) 3368-3377
    • (2002) Nucl. Acids Res. , vol.30 , pp. 3368-3377
    • Regalia, M.1    Rosenblad, M.A.2    Samuelsson, T.3
  • 23
    • 10044295145 scopus 로고    scopus 로고
    • Identification of an RNA-binding domain in human SRP72
    • Iakhiaeva E., Yin J., and Zwieb C. Identification of an RNA-binding domain in human SRP72. J. Mol. Biol. 345 (2005) 659-666
    • (2005) J. Mol. Biol. , vol.345 , pp. 659-666
    • Iakhiaeva, E.1    Yin, J.2    Zwieb, C.3
  • 24
    • 0028129127 scopus 로고
    • Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression
    • Brown J.D., Hann B.C., Medzihradszky K.F., Niwa M., Burlingame A.L., and Walter P. Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J. 13 (1994) 4390-4400
    • (1994) EMBO J. , vol.13 , pp. 4390-4400
    • Brown, J.D.1    Hann, B.C.2    Medzihradszky, K.F.3    Niwa, M.4    Burlingame, A.L.5    Walter, P.6
  • 25
    • 0036510779 scopus 로고    scopus 로고
    • Intragenic promoter adaptation and facilitated RNA polymerase III recycling in the transcription of SCR1, the 7SL RNA gene of Saccharomyces cerevisiae
    • Dieci G., Giuliodori S., Catellani M., Percudani R., and Ottonello S. Intragenic promoter adaptation and facilitated RNA polymerase III recycling in the transcription of SCR1, the 7SL RNA gene of Saccharomyces cerevisiae. J. Biol. Chem. 277 (2002) 6903-6914
    • (2002) J. Biol. Chem. , vol.277 , pp. 6903-6914
    • Dieci, G.1    Giuliodori, S.2    Catellani, M.3    Percudani, R.4    Ottonello, S.5
  • 26
    • 33744491020 scopus 로고    scopus 로고
    • Protein SRP68 of human signal recognition particle: identification of the RNA and SRP72 binding domains
    • Iakhiaeva E., Bhuiyan S.H., Yin J., and Zwieb C. Protein SRP68 of human signal recognition particle: identification of the RNA and SRP72 binding domains. Protein Sci. 15 (2006) 1290-1302
    • (2006) Protein Sci. , vol.15 , pp. 1290-1302
    • Iakhiaeva, E.1    Bhuiyan, S.H.2    Yin, J.3    Zwieb, C.4
  • 27
    • 0026529291 scopus 로고
    • Random mutagenesis of Schizosaccharomyces pombe SRP RNA: lethal and conditional lesions cluster in presumptive protein binding sites
    • Liao X., Selinger D., Althoff S., Chiang A., Hamilton D., Ma M., and Wise J.A. Random mutagenesis of Schizosaccharomyces pombe SRP RNA: lethal and conditional lesions cluster in presumptive protein binding sites. Nucl. Acids Res. 20 (1992) 1607-1615
    • (1992) Nucl. Acids Res. , vol.20 , pp. 1607-1615
    • Liao, X.1    Selinger, D.2    Althoff, S.3    Chiang, A.4    Hamilton, D.5    Ma, M.6    Wise, J.A.7
  • 28
    • 0034687215 scopus 로고    scopus 로고
    • Nuclear export of yeast signal recognition particle lacking Srp54p via the Xpo1p/Crm1p, NES-dependent pathway
    • Ciufo L.F., and Brown J.D. Nuclear export of yeast signal recognition particle lacking Srp54p via the Xpo1p/Crm1p, NES-dependent pathway. Curr. Biol. 10 (2000) 1256-1264
    • (2000) Curr. Biol. , vol.10 , pp. 1256-1264
    • Ciufo, L.F.1    Brown, J.D.2
  • 29
    • 0035858874 scopus 로고    scopus 로고
    • Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p- mediated export
    • Grosshans H., Deinert K., Hurt E., and Simos G. Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p- mediated export. J. Cell Biol. 153 (2001) 745-762
    • (2001) J. Cell Biol. , vol.153 , pp. 745-762
    • Grosshans, H.1    Deinert, K.2    Hurt, E.3    Simos, G.4
  • 30
    • 0023788988 scopus 로고
    • Internal sequences that distinguish yeast from metazoan U2 snRNA are unnecessary for pre-mRNA splicing
    • Igel A.H., and Ares Jr. M. Internal sequences that distinguish yeast from metazoan U2 snRNA are unnecessary for pre-mRNA splicing. Nature 334 (1988) 450-453
    • (1988) Nature , vol.334 , pp. 450-453
    • Igel, A.H.1    Ares Jr., M.2
  • 31
    • 0024280931 scopus 로고
    • Two conserved domains of yeast U2 snRNA are separated by 945 nonessential nucleotides
    • Shuster E.O., and Guthrie C. Two conserved domains of yeast U2 snRNA are separated by 945 nonessential nucleotides. Cell 55 (1988) 41-48
    • (1988) Cell , vol.55 , pp. 41-48
    • Shuster, E.O.1    Guthrie, C.2
  • 32
    • 0025187925 scopus 로고
    • Universally conserved and yeast-specific U1 snRNA sequences are important but not essential for U1 snRNP function
    • Liao X.L., Kretzner L., Seraphin B., and Rosbash M. Universally conserved and yeast-specific U1 snRNA sequences are important but not essential for U1 snRNP function. Genes Dev. 4 (1990) 1766-1774
    • (1990) Genes Dev. , vol.4 , pp. 1766-1774
    • Liao, X.L.1    Kretzner, L.2    Seraphin, B.3    Rosbash, M.4
  • 33
    • 0026410580 scopus 로고
    • More than half of yeast U1 snRNA is dispensable for growth
    • Siliciano P.G., Kivens W.J., and Guthrie C. More than half of yeast U1 snRNA is dispensable for growth. Nucl. Acids Res. 19 (1991) 6367-6372
    • (1991) Nucl. Acids Res. , vol.19 , pp. 6367-6372
    • Siliciano, P.G.1    Kivens, W.J.2    Guthrie, C.3
  • 34
    • 4644306171 scopus 로고    scopus 로고
    • Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain
    • Huck L., Scherrer A., Terzi L., Johnson A.E., Bernstein H.D., Cusack S., et al. Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain. Nucl. Acids Res. 32 (2004) 4915-4924
    • (2004) Nucl. Acids Res. , vol.32 , pp. 4915-4924
    • Huck, L.1    Scherrer, A.2    Terzi, L.3    Johnson, A.E.4    Bernstein, H.D.5    Cusack, S.6
  • 35
    • 0025949923 scopus 로고
    • The signal recognition particle in S. cerevisiae
    • Hann B.C., and Walter P. The signal recognition particle in S. cerevisiae. Cell 67 (1991) 131-144
    • (1991) Cell , vol.67 , pp. 131-144
    • Hann, B.C.1    Walter, P.2
  • 36
    • 0034423411 scopus 로고    scopus 로고
    • RNA helicase dynamics in pre-mRNA splicing
    • Schwer B., and Meszaros T. RNA helicase dynamics in pre-mRNA splicing. EMBO J. 19 (2000) 6582-6591
    • (2000) EMBO J. , vol.19 , pp. 6582-6591
    • Schwer, B.1    Meszaros, T.2
  • 37
    • 0033047503 scopus 로고    scopus 로고
    • Splicing factor Prp8 governs U4/U6 RNA unwinding during activation of the spliceosome
    • Kuhn A.N., Li Z., and Brow D.A. Splicing factor Prp8 governs U4/U6 RNA unwinding during activation of the spliceosome. Mol. Cell 3 (1999) 65-75
    • (1999) Mol. Cell , vol.3 , pp. 65-75
    • Kuhn, A.N.1    Li, Z.2    Brow, D.A.3
  • 38
    • 0344172814 scopus 로고    scopus 로고
    • A conditional U5 snRNA mutation affecting pre-mRNA splicing and nuclear pre-mRNA retention identifies SSD1/SRK1 as a general splicing mutant suppressor
    • Luukkonen B.G., and Seraphin B. A conditional U5 snRNA mutation affecting pre-mRNA splicing and nuclear pre-mRNA retention identifies SSD1/SRK1 as a general splicing mutant suppressor. Nucl. Acids Res. 27 (1999) 3455-3465
    • (1999) Nucl. Acids Res. , vol.27 , pp. 3455-3465
    • Luukkonen, B.G.1    Seraphin, B.2
  • 39
    • 0029871680 scopus 로고    scopus 로고
    • Identification of novel genes required for yeast pre-mRNA splicing by means of cold-sensitive mutations
    • Noble S.M., and Guthrie C. Identification of novel genes required for yeast pre-mRNA splicing by means of cold-sensitive mutations. Genetics 143 (1996) 67-80
    • (1996) Genetics , vol.143 , pp. 67-80
    • Noble, S.M.1    Guthrie, C.2
  • 40
    • 0027273672 scopus 로고
    • A cold-sensitive mutation in 16S rRNA provides evidence for helical switching in ribosome assembly
    • Dammel C.S., and Noller H.F. A cold-sensitive mutation in 16S rRNA provides evidence for helical switching in ribosome assembly. Genes Dev. 7 (1993) 660-670
    • (1993) Genes Dev. , vol.7 , pp. 660-670
    • Dammel, C.S.1    Noller, H.F.2
  • 42
    • 0037044315 scopus 로고    scopus 로고
    • Isolation and characterization of a family of stable RNA tetraloops with the motif YNMG that participate in tertiary interactions
    • Proctor D.J., Schaak J.E., Bevilacqua J.M., Falzone C.J., and Bevilacqua P.C. Isolation and characterization of a family of stable RNA tetraloops with the motif YNMG that participate in tertiary interactions. Biochemistry 41 (2002) 12062-12075
    • (2002) Biochemistry , vol.41 , pp. 12062-12075
    • Proctor, D.J.1    Schaak, J.E.2    Bevilacqua, J.M.3    Falzone, C.J.4    Bevilacqua, P.C.5
  • 43
    • 0037461336 scopus 로고    scopus 로고
    • Extending the family of UNCG-like tetraloop motifs: NMR structure of a CACG tetraloop from coxsackievirus B3
    • Du Z., Yu J., Andino R., and James T.L. Extending the family of UNCG-like tetraloop motifs: NMR structure of a CACG tetraloop from coxsackievirus B3. Biochemistry 42 (2003) 4373-4383
    • (2003) Biochemistry , vol.42 , pp. 4373-4383
    • Du, Z.1    Yu, J.2    Andino, R.3    James, T.L.4


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