References:

[1] Keenan, R. J.; Freymann, D. M.; Walter, P. and Stroud, R. M. (1998): Crystal structure of the signal sequence binding subunit of the signal recognition particle, Cell, (vol. 94), No. 2, pp.181-91..

[2] Blobel, G and Sabatini, DD (1971): Ribosome-membrane interaction in eucaryotic cells, Biomembranes, pp.193-195.

[3] Walter, P.; Ibrahimi, I. and Blobel, G. (1981): Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein, J Cell Biol, (vol. 91), No. 2 Pt 1, pp.545-50..

[4] Koch, H. G.; Moser, M. and Muller, M. (2003): Signal recognition particle-dependent protein targeting, universal to all kingdoms of life, Rev Physiol Biochem Pharmacol, (vol. 146:55-94.), No. 10.

[5] Gundelfinger, E. D.; Krause, E.; Melli, M. and Dobberstein, B. (1983): The organization of the 7SL RNA in the signal recognition particle, Nucleic Acids Res, (vol. 11), No. 21, pp.7363-74..

[6] Siegel, V. and Walter, P. (1988): Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: analysis of biochemical mutants of SRP, Cell, (vol. 52), No. 1, pp.39-49..

[7] Walter, P. and Blobel, G. (1983): Disassembly and reconstitution of signal recognition particle, Cell, (vol. 34), No. 2, pp.525-33..

[8] Connolly, T. and Gilmore, R. (1989): The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide, Cell, (vol. 57), No. 4, pp.599-610..

[9] Bernstein, H. D.; Poritz, M. A.; Strub, K.; Hoben, P. J.; Brenner, S. and Walter, P. (1989): Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle, Nature, (vol. 340), No. 6233, pp.482-6..

[10] Romisch, K.; Webb, J.; Lingelbach, K.; Gausepohl, H. and Dobberstein, B. (1990): The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain, J Cell Biol, (vol. 111), No. 5 Pt 1, pp.1793-802..

[11] Batey, R. T.; Rambo, R. P.; Lucast, L.; Rha, B. and Doudna, J. A. (2000): Crystal structure of the ribonucleoprotein core of the signal recognition particle, Science, (vol. 287), No. 5456, pp.1232-9..

[12] Zopf, D.; Bernstein, H. D.; Johnson, A. E. and Walter, P. (1990): 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, (vol. 9), No. 13, pp.4511-7..

[13] Pool, M. R.; Stumm, J.; Fulga, T. A.; Sinning, I. and Dobberstein, B. (2002): Distinct modes of signal recognition particle interaction with the ribosome, Science, (vol. 297), No. 5585, pp.1345-8..

[14] Siegel, V. and Walter, P. (1986): Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact, Nature, (vol. 320), No. 6057, pp.81-4..

[15] Walter, P. and Blobel, G. (1981): Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes, J Cell Biol, (vol. 91), No. 2 Pt 1, pp.557-61..

[16] Wolin, S. L. and Walter, P. (1989): Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate, J Cell Biol, (vol. 109), No. 6 Pt 1, pp.2617-22..

[17] Mason, N.; Ciufo, L. F. and Brown, J. D. (2000): Elongation arrest is a physiologically important function of signal recognition particle, Embo J, (vol. 19), No. 15, pp.4164-74..

[18] Siegel, V. and Walter, P. (1985): Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane, J Cell Biol, (vol. 100), No. 6, pp.1913-21..

[19] Zheng, N. and Gierasch, L. M. (1997): Domain interactions in E. coli SRP: stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain, Mol Cell, (vol. 1), No. 1, pp.79-87..

[20] Cleverley, R. M.; Zheng, N. and Gierasch, L. M. (2001): The cost of exposing a hydrophobic loop and implications for the functional role of 4.5 S RNA in the Escherichia coli signal recognition particle, J Biol Chem, (vol. 276), No. 22, pp.19327-31.

[21] Larsen, N. and Zwieb, C. (1991): SRP-RNA sequence alignment and secondary structure, Nucleic Acids Res, (vol. 19), No. 2, pp.209-15..

[22] Poritz, M. A.; Strub, K. and Walter, P. (1988): Human SRP RNA and E. coli 4.5S RNA contain a highly homologous structural domain, Cell, (vol. 55), No. 1, pp.4-6..

[23] Honda, K.; Nakamura, K.; Nishiguchi, M. and Yamane, K. (1993): Cloning and characterization of a Bacillus subtilis gene encoding a homolog of the 54-kilodalton subunit of mammalian signal recognition particle and Escherichia coli Ffh, J Bacteriol, (vol. 175), No. 15, pp.4885-94..

[24] Nakamura, K.; Yahagi, S.; Yamazaki, T. and Yamane, K. (1999): Bacillus subtilis histone-like protein, HBsu, is an integral component of a SRP-like particle that can bind the Alu domain of small cytoplasmic RNA, J Biol Chem, (vol. 274), No. 19, pp.13569-76..

[25] Wild, K.; Weichenrieder, O.; Strub, K.; Sinning, I. and Cusack, S. (2002): Towards the structure of the mammalian signal recognition particle, Curr Opin Struct Biol, (vol. 12), No. 1, pp.72-81..

[26] Keenan, R. J.; Freymann, D. M.; Stroud, R. M. and Walter, P. (2001): The signal recognition particle, Annu Rev Biochem, (vol. 70:755-75.), No. 52.

[27] Bhuiyan, S. H.; Gowda, K.; Hotokezaka, H. and Zwieb, C. (2000): Assembly of archaeal signal recognition particle from recombinant components, Nucleic Acids Res, (vol. 28), No. 6, pp.1365-73.

[28] Van Nues, R. W. and Brown, J. D. (2004): Saccharomyces SRP RNA secondary structures: a conserved S-domain and extended Alu-domain, Rna, (vol. 10), No. 1, pp.75-89.

[29] Bernstein, H. D.; Zopf, D.; Freymann, D. M. and Walter, P. (1993): Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog, Proc Natl Acad Sci U S A, (vol. 90), No. 11, pp.5229-33..

[30] Schuenemann, D.; Gupta, S.; Persello-Cartieaux, F.; Klimyuk, Vi Vi; Jones, J. D. G.; Nussaume, L. and Hoffman, N. E. (1998): A novel signal recognition particle targets light-harvesting proteins to the thylakoid membranes, Proc Natl Acad Sci U S A, (vol. 95), No. 17, pp.10312-6.

[31] Eichacker, L. A. and Henry, R. (2001): Function of a chloroplast SRP in thylakoid protein export, Biochim Biophys Acta, (vol. 1541), No. 1-2, pp.120-34.

[32] Zhang, L.; Paakkarinen, V.; van Wijk, K. J. and Aro, E. M. (1999): Co-translational assembly of the D1 protein into photosystem II, J Biol Chem, (vol. 274), No. 23, pp.16062-7.

[33] Zhang, L.; Paakkarinen, V.; Suorsa, M. and Aro, E. M. (2001): A SecY homologue is involved in chloroplast-encoded D1 protein biogenesis, J Biol Chem, (vol. 276), No. 41, pp.37809-14.

[34] Nilsson, R.; Brunner, J.; Hoffman, N. E. and van Wijk, K. J. (1999): Interactions of ribosome nascent chain complexes of the chloroplast-encoded D1 thylakoid membrane protein with cpSRP54, Embo J, (vol. 18), No. 3, pp.733-42.

[35] Li, X.; Henry, R.; Yuan, J.; Cline, K. and Hoffman, N. E. (1995): A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the posttranslational integration of a protein into thylakoid membranes, Proc Natl Acad Sci U S A, (vol. 92), No. 9, pp.3789-93.

[36] Groves, M. R.; Mant, A.; Kuhn, A.; Koch, J.; Dubel, S.; Robinson, C. and Sinning, I. (2001): Functional characterization of recombinant chloroplast signal recognition particle, J Biol Chem, (vol. 276), No. 30, pp.27778-86.

[37] Politz, J. C.; Yarovoi, S.; Kilroy, S. M.; Gowda, K.; Zwieb, C. and Pederson, T. (2000): Signal recognition particle components in the nucleolus, Proc Natl Acad Sci U S A, (vol. 97), No. 1, pp.55-60..

[38] Grosshans, H.; Deinert, K.; Hurt, E. and Simos, G. (2001): 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, (vol. 153), No. 4, pp.745-62..

[39] Strub, K. and Walter, P. (1990): Assembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNA, Mol Cell Biol, (vol. 10), No. 2, pp.777-84..

[40] Weichenrieder, O.; Wild, K.; Strub, K. and Cusack, S. (2000): Structure and assembly of the Alu domain of the mammalian signal recognition particle, Nature, (vol. 408), No. 6809, pp.167-73..

[41] Chen, Y.; Sinha, K.; Perumal, K.; Gu, J. and Reddy, R. (1998): Accurate 3' end processing and adenylation of human signal recognition particle RNA and alu RNA in vitro, J Biol Chem, (vol. 273), No. 52, pp.35023-31.

[42] Emde, G.; Frontzek, A. and Benecke, B. J. (1997): Secondary structure of the nascent 7S L RNA mediates efficient transcription by RNA polymerase III, Rna, (vol. 3), No. 5, pp.538-49.

[43] Weiner, A. M.; Deininger, P. L. and Efstratiadis, A. (1986): Nonviral retroposons: genes, pseudogenes, and transposable elements generated by the reverse flow of genetic information, Annu Rev Biochem, (vol. 55), pp.631-61.

[44] Mighell, A. J.; Markham, A. F. and Robinson, P. A. (1997): Alu sequences, FEBS Lett, (vol. 417), No. 1, pp.1-5.

[45] Wild, K.; Sinning, I. and Cusack, S. (2001): Crystal structure of an early protein-RNA assembly complex of the signal recognition particle, Science, (vol. 294), No. 5542, pp.598-601..

[46] Kuglstatter, A.; Oubridge, C. and Nagai, K. (2002): Induced structural changes of 7SL RNA during the assembly of human signal recognition particle, Nat Struct Biol, (vol. 9), No. 10, pp.740-4.

[47] Nagai, K.; Oubridge, C.; Kuglstatter, A.; Menichelli, E.; Isel, C. and Jovine, L. (2003): Structure, function and evolution of the signal recognition particle, Embo J, (vol. 22), No. 14, pp.3479-85..

[48] Lutcke, H.; Prehn, S.; Ashford, A. J.; Remus, M.; Frank, R. and Dobberstein, B. (1993): Assembly of the 68- and 72-kD proteins of signal recognition particle with 7S RNA, J Cell Biol, (vol. 121), No. 5, pp.977-85..

[49] Siegel, V. and Walter, P. (1988): Binding sites of the 19-kDa and 68/72-kDa signal recognition particle (SRP) proteins on SRP RNA as determined in protein-RNA "footprinting", Proc Natl Acad Sci U S A, (vol. 85), No. 6, pp.1801-5..

[50] Althoff, S.; Selinger, D. and Wise, J. A. (1994): Molecular evolution of SRP cycle components: functional implications, Nucleic Acids Res, (vol. 22), No. 11, pp.1933-47..

[51] Gellman, S. H. (1991): On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces, Biochemistry, (vol. 30), No. 27, pp.6633-6.

[52] Luirink, J.; High, S.; Wood, H.; Giner, A.; Tollervey, D. and Dobberstein, B. (1992): Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex, Nature, (vol. 359), No. 6397, pp.741-3..

[53] Rosendal, K. R.; Wild, K.; Montoya, G. and Sinning, I. (2003): Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication, Proc Natl Acad Sci U S A, (vol. 100), No. 25, pp.14701-6.

[54] Schmitz, U.; James, T. L.; Lukavsky, P. and Walter, P. (1999): Structure of the most conserved internal loop in SRP RNA, Nat Struct Biol, (vol. 6), No. 7, pp.634-8..

[55] Yaver, D. S.; Matoba, S. and Ogrydziak, D. M. (1992): A mutation in the signal recognition particle 7S RNA of the yeast Yarrowia lipolytica preferentially affects synthesis of the alkaline extracellular protease: in vivo evidence for translational arrest, J Cell Biol, (vol. 116), No. 3, pp.605-16.

[56] Raine, A.; Ullers, R.; Pavlov, M.; Luirink, J.; Wikberg, J. E. and Ehrenberg, M. (2003): Targeting and insertion of heterologous membrane proteins in E. coli, Biochimie, (vol. 85), No. 7, pp.659-68.

[57] Gilmore, R.; Blobel, G. and Walter, P. (1982): Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle, J Cell Biol, (vol. 95), No. 2 Pt 1, pp.463-9..

[58] Young, J. C. and Andrews, D. W. (1996): The signal recognition particle receptor alpha subunit assembles co-translationally on the endoplasmic reticulum membrane during an mRNA-encoded translation pause in vitro, Embo J, (vol. 15), No. 1, pp.172-81..

[59] Bourne, H. R.; Sanders, D. A. and McCormick, F. (1990): The GTPase superfamily: a conserved switch for diverse cell functions, Nature, (vol. 348), No. 6297, pp.125-32.

[60] Millman, J. S. and Andrews, D. W. (1997): Switching the model: a concerted mechanism for GTPases in protein targeting, Cell, (vol. 89), No. 5, pp.673-6.

[61] Montoya, G.; Svensson, C.; Luirink, J. and Sinning, I. (1997): Crystal structure of the NG domain from the signal-recognition particle receptor FtsY, Nature, (vol. 385), No. 6614, pp.365-8..

[62] Freymann, D. M.; Keenan, R. J.; Stroud, R. M. and Walter, P. (1997): Structure of the conserved GTPase domain of the signal recognition particle, Nature, (vol. 385), No. 6614, pp.361-4..

[63] Miller, J. D.; Wilhelm, H.; Gierasch, L.; Gilmore, R. and Walter, P. (1993): GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation, Nature, (vol. 366), No. 6453, pp.351-4..

[64] Miller, J. D.; Bernstein, H. D. and Walter, P. (1994): Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor, Nature, (vol. 367), No. 6464, pp.657-9..

[65] Moser, C.; Mol, O.; Goody, R. S. and Sinning, I. (1997): The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain, Proc Natl Acad Sci U S A, (vol. 94), No. 21, pp.11339-44..

[66] Jagath, J. R.; Rodnina, M. V.; Lentzen, G. and Wintermeyer, W. (1998): Interaction of guanine nucleotides with the signal recognition particle from Escherichia coli, Biochemistry, (vol. 37), No. 44, pp.15408-13..

[67] Newitt, J. A. and Bernstein, H. D. (1997): The N-domain of the signal recognition particle 54-kDa subunit promotes efficient signal sequence binding, Eur J Biochem, (vol. 245), No. 3, pp.720-9.

[68] Zopf, D.; Bernstein, H. D. and Walter, P. (1993): GTPase domain of the 54-kD subunit of the mammalian signal recognition particle is required for protein translocation but not for signal sequence binding, J Cell Biol, (vol. 120), No. 5, pp.1113-21..

[69] Peluso, P.; Herschlag, D.; Nock, S.; Freymann, D. M.; Johnson, A. E. and Walter, P. (2000): Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor, Science, (vol. 288), No. 5471, pp.1640-3..

[70] Jagath, J. R.; Matassova, N. B.; de Leeuw, E.; Warnecke, J. M.; Lentzen, G.; Rodnina, M. V.; Luirink, J. and Wintermeyer, W. (2001): Important role of the tetraloop region of 4.5S RNA in SRP binding to its receptor FtsY, Rna, (vol. 7), No. 2, pp.293-301..

[71] Bacher, G.; Lutcke, H.; Jungnickel, B.; Rapoport, T. A. and Dobberstein, B. (1996): Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting, Nature, (vol. 381), No. 6579, pp.248-51..

[72] de Leeuw, E.; Poland, D.; Mol, O.; Sinning, I.; ten Hagen-Jongman, C. M.; Oudega, B. and Luirink, J. (1997): Membrane association of FtsY, the E. coli SRP receptor, FEBS Lett, (vol. 416), No. 3, pp.225-9..

[73] de Leeuw, E.; te Kaat, K.; Moser, C.; Menestrina, G.; Demel, R.; de Kruijff, B.; Oudega, B.; Luirink, J. and Sinning, I. (2000): Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity, Embo J, (vol. 19), No. 4, pp.531-41.

[74] Song, W.; Raden, D.; Mandon, E. C. and Gilmore, R. (2000): Role of Sec61alpha in the regulated transfer of the ribosome-nascent chain complex from the signal recognition particle to the translocation channel, Cell, (vol. 100), No. 3, pp.333-43.

[75] Shepotinovskaya, I. V. and Freymann, D. M. (2002): Conformational change of the N-domain on formation of the complex between the GTPase domains of Thermus aquaticus Ffh and FtsY, Biochim Biophys Acta, (vol. 1597), No. 1, pp.107-14..

[76] Powers, T. and Walter, P. (1995): Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases, Science, (vol. 269), No. 5229, pp.1422-4.

[77] Focia, P. J.; Shepotinovskaya, I. V.; Seidler, J. A. and Freymann, D. M. (2004): Heterodimeric GTPase core of the SRP targeting complex, Science, (vol. 303), No. 5656, pp.373-7.

[78] Egea, P. F.; Shan, S. O.; Napetschnig, J.; Savage, D. F.; Walter, P. and Stroud, R. M. (2004): Substrate twinning activates the signal recognition particle and its receptor, Nature, (vol. 427), No. 6971, pp.215-21.

[79] Shan, S. O.; Stroud, R. M. and Walter, P. (2004): Mechanism of association and reciprocal activation of two GTPases, PLoS Biol, (vol. 2), No. 10, p. e320.

[80] Caldon, C. E.; Yoong, P. and March, P. E. (2001): Evolution of a molecular switch: universal bacterial GTPases regulate ribosome function, Mol Microbiol, (vol. 41), No. 2, pp.289-97.

[81] Schwartz, T. and Blobel, G. (2003): Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor, Cell, (vol. 112), No. 6, pp.793-803..

[82] Legate, K. R.; Falcone, D. and Andrews, D. W. (2000): Nucleotide-dependent binding of the GTPase domain of the signal recognition particle receptor beta-subunit to the alpha-subunit, J Biol Chem, (vol. 275), No. 35, pp.27439-46..

[83] Helmers, J.; Schmidt, D.; Glavy, J. S.; Blobel, G. and Schwartz, T. (2003): The beta-subunit of the protein-conducting channel of the endoplasmic reticulum functions as the guanine nucleotide exchange factor for the beta-subunit of the signal recognition particle receptor, J Biol Chem, (vol. 278), No. 26, pp.23686-90.

[84] Bacher, G.; Pool, M. and Dobberstein, B. (1999): The ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptor, J Cell Biol, (vol. 146), No. 4, pp.723-30..

[85] Fulga, T. A.; Sinning, I.; Dobberstein, B. and Pool, M. R. (2001): SRbeta coordinates signal sequence release from SRP with ribosome binding to the translocon, Embo J, (vol. 20), No. 9, pp.2338-47..

[86] Martoglio, B.; Hauser, S. and Dobberstein, B. (1997), Celis, J.C., Ed, Cell Biology: A Laboratory Handbook (Vol. 34), pp. 265-273., Academic Press, San Diego.

[87] Walter, P. and Blobel, G. (1983): Signal recognition particle: a ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties, Methods Enzymol, (vol. 96), pp.682-91..

[88] Wagenknecht, T.; Grassucci, R. and Frank, J. (1988): Electron microscopy and computer image averaging of ice-embedded large ribosomal subunits from Escherichia coli, J Mol Biol, (vol. 199), No. 1, pp.137-47..

[89] Frank, J.; Radermacher, M.; Penczek, P.; Zhu, J.; Li, Y.; Ladjadj, M. and Leith, A. (1996): SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields, J Struct Biol, (vol. 116), No. 1, pp.190-9.

[90] Mindell, J. A. and Grigorieff, N. (2003): Accurate determination of local defocus and specimen tilt in electron microscopy, J Struct Biol, (vol. 142), No. 3, pp.334-47.

[91] Roseman, A. M. (2003): Particle finding in electron micrographs using a fast local correlation algorithm, Ultramicroscopy, (vol. 94), No. 3-4, pp.225-36.

[92] Jones, T.A.; Zhou, J.Y.; Cowan, S.W. and Kjeldgaard, M. (1991): Improved methods for building protein models in electron density maps and the location of errors in these models., Acta Crystallogr. A, (vol. A47), pp.110-119.

[93] Huang, Q.; Abdulrahman, S.; Yin, J. and Zwieb, C. (2002): Systematic site-directed mutagenesis of human protein SRP54: interactions with signal recognition particle RNA and modes of signal peptide recognition, Biochemistry, (vol. 41), No. 38, pp.11362-71..

[94] Padmanabhan, S. and Freymann, D. M. (2001): The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPase, Structure (Camb), (vol. 9), No. 9, pp.859-67..

[95] Rosenblad, M. A.; Gorodkin, J.; Knudsen, B.; Zwieb, C. and Samuelsson, T. (2003): SRPDB: Signal Recognition Particle Database, Nucleic Acids Res, (vol. 31), No. 1, pp.363-4. 12:.

[96] Rath, B. K.; Hegerl, R.; Leith, A.; Shaikh, T. R.; Wagenknecht, T. and Frank, J. (2003): Fast 3D motif search of EM density maps using a locally normalized cross-correlation function, J Struct Biol, (vol. 144), No. 1-2, pp.95-103.

[97] Chao, J. A.; Prasad, G. S.; White, S. A.; Stout, C. D. and Williamson, J. R. (2003): Inherent protein structural flexibility at the RNA-binding interface of L30e, J Mol Biol, (vol. 326), No. 4, pp.999-1004.

[98] Walter, P. and Blobel, G. (1983): Subcellular distribution of signal recognition particle and 7SL-RNA determined with polypeptide-specific antibodies and complementary DNA probe, J Cell Biol, (vol. 97), No. 6, pp.1693-9..

[99] Beckmann, R.; Spahn, C. M.; Eswar, N.; Helmers, J.; Penczek, P. A.; Sali, A.; Frank, J. and Blobel, G. (2001): Architecture of the protein-conducting channel associated with the translating 80S ribosome, Cell, (vol. 107), No. 3, pp.361-72.

[100] Spahn, C. M.; Beckmann, R.; Eswar, N.; Penczek, P. A.; Sali, A.; Blobel, G. and Frank, J. (2001): Structure of the 80S ribosome from Saccharomyces cerevisiae--tRNA-ribosome and subunit-subunit interactions, Cell, (vol. 107), No. 3, pp.373-86.

[101] 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, (vol. 289), No. 5481, pp.905-20.

[102] Thomas, Y.; Bui, N. and Strub, K. (1997): 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, Nucleic Acids Res, (vol. 25), No. 10, pp.1920-9..

[103] Gu, S. Q.; Peske, F.; Wieden, H. J.; Rodnina, M. V. and Wintermeyer, W. (2003): The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome, Rna, (vol. 9), No. 5, pp.566-73..

[104] Eisner, G.; Koch, H. G.; Beck, K.; Brunner, J. and Muller, M. (2003): Ligand crowding at a nascent signal sequence, J Cell Biol, (vol. 163), No. 1, pp.35-44.

[105] Kramer, G.; Rauch, T.; Rist, W.; Vorderwulbecke, S.; Patzelt, H.; Schulze-Specking, A.; Ban, N.; Deuerling, E. and Bukau, B. (2002): L23 protein functions as a chaperone docking site on the ribosome, Nature, (vol. 419), No. 6903, pp.171-4.

[106] Ullers, R. S.; Houben, E. N.; Raine, A.; ten Hagen-Jongman, C. M.; Ehrenberg, M.; Brunner, J.; Oudega, B.; Harms, N. and Luirink, J. (2003): Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome, J Cell Biol, (vol. 161), No. 4, pp.679-84..

[107] Rinke-Appel, J.; Osswald, M.; von Knoblauch, K.; Mueller, F.; Brimacombe, R.; Sergiev, P.; Avdeeva, O.; Bogdanov, A. and Dontsova, O. (2002): Crosslinking of 4.5S RNA to the Escherichia coli ribosome in the presence or absence of the protein Ffh, Rna, (vol. 8), No. 5, pp.612-25..

[108] Diener, J. L. and Wilson, C. (2000): Role of SRP19 in assembly of the Archaeoglobus fulgidus signal recognition particle, Biochemistry, (vol. 39), No. 42, pp.12862-74.

[109] Esnouf, R. M. (1997): An extensively modified version of MolScript that includes greatly enhanced coloring capabilities, J Mol Graph Model, (vol. 15), No. 2, pp.132-4, 112-3.

[110] Merritt and Bacon (1997): Raster 3D, Macromolecular Crystallography, (vol. 277), No. 277, pp.505-524..

[111] Cleverley, R. M. and Gierasch, L. M. (2002): Mapping the signal sequence-binding site on SRP reveals a significant role for the NG domain, J Biol Chem, (vol. 277), No. 48, pp.46763-8.

[112] Eng, F. J. and Warner, J. R. (1991): Structural basis for the regulation of splicing of a yeast messenger RNA, Cell, (vol. 65), No. 5, pp.797-804.

[113] Vilardell, J. and Warner, J. R. (1994): Regulation of splicing at an intermediate step in the formation of the spliceosome, Genes Dev, (vol. 8), No. 2, pp.211-20.

[114] Dabeva, M. D. and Warner, J. R. (1993): Ribosomal protein L32 of Saccharomyces cerevisiae regulates both splicing and translation of its own transcript, J Biol Chem, (vol. 268), No. 26, pp.19669-74.

[115] Li, B.; Vilardell, J. and Warner, J. R. (1996): An RNA structure involved in feedback regulation of splicing and of translation is critical for biological fitness, Proc Natl Acad Sci U S A, (vol. 93), No. 4, pp.1596-600.

[116] Vilardell, J.; Yu, S. J. and Warner, J. R. (2000): Multiple functions of an evolutionarily conserved RNA binding domain, Mol Cell, (vol. 5), No. 4, pp.761-6.

[117] Chen, Y. W.; Bycroft, M. and Wong, K. B. (2003): Crystal structure of ribosomal protein L30e from the extreme thermophile Thermococcus celer: thermal stability and RNA binding, Biochemistry, (vol. 42), No. 10, pp.2857-65.

[118] Bates, P. A.; Kelley, L. A.; MacCallum, R. M. and Sternberg, M. J. (2001): Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM, Proteins, (vol. Suppl 5), pp.39-46.

[119] Baronas-Lowell, D. M. and Warner, J. R. (1990): Ribosomal protein L30 is dispensable in the yeast Saccharomyces cerevisiae, Mol Cell Biol, (vol. 10), No. 10, pp.5235-43.

[120] Spahn, C. M.; Gomez-Lorenzo, M. G.; Grassucci, R. A.; Jorgensen, R.; Andersen, G. R.; Beckmann, R.; Penczek, P. A.; Ballesta, J. P. and Frank, J. (2004): Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation, Embo J, (vol. 23), No. 5, pp.1008-1019.

[121] Andrews, D. W.; Walter, P. and Ottensmeyer, F. P. (1987): Evidence for an extended 7SL RNA structure in the signal recognition particle, Embo J, (vol. 6), No. 11, pp.3471-7.

[122] Morgan, D. G.; Menetret, J. F.; Neuhof, A.; Rapoport, T. A. and Akey, C. W. (2002): Structure of the mammalian ribosome-channel complex at 17A resolution, J Mol Biol, (vol. 324), No. 4, pp.871-86.

[123] Moller, I.; Jung, M.; Beatrix, B.; Levy, R.; Kreibich, G.; Zimmermann, R.; Wiedmann, M. and Lauring, B. (1998): A general mechanism for regulation of access to the translocon: competition for a membrane attachment site on ribosomes, Proc Natl Acad Sci U S A, (vol. 95), No. 23, pp.13425-30.

[124] Wilson, D. N.; Blaha, G.; Connell, S. R.; Ivanov, P. V.; Jenke, H.; Stelzl, U.; Teraoka, Y. and Nierhaus, K. H. (2002): Protein synthesis at atomic resolution: mechanistics of translation in the light of highly resolved structures for the ribosome, Curr Protein Pept Sci, (vol. 3), No. 1, pp.1-53.

[125] Gomez-Lorenzo, M. G.; Spahn, C. M.; Agrawal, R. K.; Grassucci, R. A.; Penczek, P.; Chakraburtty, K.; Ballesta, J. P.; Lavandera, J. L.; Garcia-Bustos, J. F. and Frank, J. (2000): Three-dimensional cryo-electron microscopy localization of EF2 in the Saccharomyces cerevisiae 80S ribosome at 17.5 A resolution, Embo J, (vol. 19), No. 11, pp.2710-8.

[126] Spahn, Christian; Gomez-Lorenzo, Maria G.; Grassucci, Robert A.; Jørgensen, Rene; Andersen, Gregers R.; Beckmann, Roland; Penczek, Pawel A.; Ballesta, Juan P. G. and Frank, Joachim: Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation, EMBO J. in press.

[127] Valle, M.; Zavialov, A.; Li, W.; Stagg, S. M.; Sengupta, J.; Nielsen, R. C.; Nissen, P.; Harvey, S. C.; Ehrenberg, M. and Frank, J. (2003): Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy, Nat Struct Biol, (vol. 10), No. 11, pp.899-906.

[128] Wolin, S. L. and Walter, P. (1988): Ribosome pausing and stacking during translation of a eukaryotic mRNA, Embo J, (vol. 7), No. 11, pp.3559-69..

[129] Ogg, S. C. and Walter, P. (1995): SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step during translation elongation, Cell, (vol. 81), No. 7, pp.1075-84..

[130] Andreazzoli, M. and Gerbi, S. A. (1991): Changes in 7SL RNA conformation during the signal recognition particle cycle, Embo J, (vol. 10), No. 4, pp.767-77.

[131] Wiedmann, M.; Kurzchalia, T. V.; Bielka, H. and Rapoport, T. A. (1987): Direct probing of the interaction between the signal sequence of nascent preprolactin and the signal recognition particle by specific cross-linking, J Cell Biol, (vol. 104), No. 2, pp.201-8..

[132] Terzi, L.; Pool, M. R.; Dobberstein, B. and Strub, K. (2004): Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognition, Biochemistry, (vol. 43), No. 1, pp.107-17.

[133] Flanagan, J. J.; Chen, J. C.; Miao, Y.; Shao, Y.; Lin, J.; Bock, P. E. and Johnson, A. E. (2003): Signal recognition particle binds to ribosome-bound signal sequences with fluorescence-detected subnanomolar affinity that does not diminish as the nascent chain lengthens, J Biol Chem, (vol. 278), No. 20, pp.18628-37.

[134] Mandon, E. C.; Jiang, Y. and Gilmore, R. (2003): Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum, J Cell Biol, (vol. 162), No. 4, pp.575-85..

[135] Wild, K.; Rosendal, KR. and I., Sinning (2004): A structural step into the SRP cycle, (vol. In press).


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