Bibliography
- · Althoff, S., Selinger, D., and Wise, J. A. (1994). Molecular evolution of SRP cycle components: functional implications. Nucleic Acids Res 22, 1933-1947.
- · Andreazzoli, M., and Gerbi, S. A. (1991). Changes in 7SL RNA conformation during the signal recognition particle cycle. Embo J 10, 767-777.
- · Andrews, D. W., Walter, P., and Ottensmeyer, F. P. (1985). Structure of the signal recognition particle by electron microscopy. Proc Natl Acad Sci U S A 82, 785-789.
- · Andrews, D. W., Walter, P., and Ottensmeyer, F. P. (1987). Evidence for an extended 7SL RNA structure in the signal recognition particle. Embo J 6, 3471-3477.
- · Arnaud, N., Cheynet, V., Oriol, G., Mandrand, B., and Mallet, F. (1997). Construction and expression of a modular gene encoding bacteriophage T7 RNA polymerase. Gene 199, 149-156.
- · Bacher, G., Lütcke, 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 (see comments). Nature 381, 248-251.
- · 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 146, 723-730.
- · 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.[comment]. Science 287, 1232-1239.
- · 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 107, 361-372.
- · Beja, O., Ullu, E., and Michaeli, S. (1993). Identification of a tRNA-like molecule that copurifies with the 7SL RNA of Trypanosoma brucei. Mol Biochem Parasitol 57, 223-229.
- · 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 340, 482-486.
- · Birse, D. E., Kapp, U., Strub, K., Cusack, S., and Aberg, A. (1997). The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14. Embo J 16, 3757-3766.
- · Blobel, G., and Dobberstein, B. (1975a). Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol 67, 835-851.
- · Blobel, G., and Dobberstein, B. (1975b). Transfer to proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J Cell Biol 67, 852-862.
- · Blobel, G., and Sabatini, D. (1971). Dissociation of mammalian polyribosomes into subunits by puromycin. Proc Natl Acad Sci U S A 68, 390-394.
- · Bourgaize, D. B., and Fournier, M. J. (1987). Initiation of translation is impaired in E. coli cells deficient in 4.5S RNA. Nature 325, 281-284.
- · Bourne, H. R., Sanders, D. A., and McCormick, F. (1991). The GTPase superfamily: conserved structure and molecular mechanism. Nature 349, 117-127.
- · Bovia, F., Bui, N., and Strub, K. (1994). The heterodimeric subunit SRP9/14 of the signal recognition particle functions as permuted single polypeptide chain. Nucleic Acids Res 22, 2028-2035.
- · Bovia, F., Fornallaz, M., Leffers, H., and Strub, K. (1995). The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs. Mol Biol Cell 6, 471-484.
- · Bovia, F., Wolff, N., Ryser, S., and Strub, K. (1997). The SRP9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog. Nucleic Acids Res 25, 318-326.
- · Brown, J., D., Hann, B. C., Medzihradszky, K. F., Niwa, M., Burlingame, A. L., and Walter, P. (1994). Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. Embo J 13, 4390-4400.
- · Brown, S. (1989). Time of action of 4.5 S RNA in Escherichia coli translation. Journal of Molecular Biology 209, 79-90.
- · Brown, S. (1991). Genes for 7S RNAs can replace the gene for 4.5S RNA in growth of Escherichia coli. Journal of Bacteriology 173, 1835-1837.
- · Brunelli, C. A., O'Connor, M., and Dahlberg, A. E. (2002). Decreased requirement for 4.5S RNA in 16S and 23S rRNA mutants of Escherichia coli. FEBS Letters 514, 44-48.
- · Bui, N., and Strub, K. (1999). New insights into signal recognition and elongation arrest activities of the signal recognition particle. Biol Chem 380, 135-145.
- · Bui, N., Wolff, N., Cusack, S., and Strub, K. (1997). Mutational analysis of the protein subunits of the signal recognition particle Alu-domain. Rna 3, 748-763.
- · Chang, D. Y., and Maraia, R. J. (1993). A cellular protein binds B1 and Alu small cytoplasmic RNAs in vitro. J Biol Chem 268, 6423-6428.
- · Chang, D.-Y., Nelson, B., Bilyeu, T., Hsu, K., Darlington, G., and Maraia, R. J. (1994). A Human Alu RNA-Binding Protein Whose Expression is Associated with Accumulation of
- · Small Cytoplasmic Alu RNA. Mol Cell Biol 14, 3949-3959.
- · Chang, D. Y., Newitt, J. A., Hsu, K., Bernstein, H. D., and Maraia, R. J. (1997). A highly conserved nucleotide in the Alu domain of SRP RNA mediates translation arrest through high affinity binding to SRP9/14. Nucleic Acids Res 25, 1117-1122.
- · Clemons, W. M., Jr., Gowda, K., Black, S. D., Zwieb, C., and Ramakrishnan, V. (1999). Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 A resolution: evidence for the mechanism of signal peptide binding. Journal of Molecular Biology 292, 697-705.
- · Conn, G. L., Draper, D. E., Lattman, E. E., and Gittis, A. G. (1999). Crystal structure of a conserved ribosomal protein-RNA complex. Science 284, 1171-1174.
- · 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 57, 599-610.
- · Connolly, T., Rapiejko, P. J., and Gilmore, R. (1991). Requirement of GTP Hydrolysis for Dissociation of the Signal Recognition Particle from Its Receptor. Science 252, 1171-1173.
- · Diener, J. L., and Wilson, C. (2000). Role of SRP19 in assembly of the Archaeoglobus fulgidus signal recognition particle. Biochemistry 39, 12862-12874.
- · Eichler, J., and Moll, R. (2001). The signal recognition particle of Archaea. Trends in Microbiology 9, 130-136.
- · England, T. E., Bruce, A. G., and Uhlenbeck, O. C. (1980). Specific labelling of 3' termini of RNA with T4 RNA ligase. Methods Enzymol 65, 65-74.
- · 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 385, 361-364.
- · Freymann, D. M., Keenan, R. J., Stroud, R. M., and Walter, P. (1999). Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP. Nat Struct Biol 6, 793-801.
- · 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 20, 2338-2347.
- · Gill, S. C., and von Hippel, P. H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182, 319-326.
- · Gilmore, R., Blobel, G., and Walter, P. (1982a). Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle. J Cell Biol 95, 463-469.
- · Gilmore, R., Walter, P., and Blobel, G. (1982b). Protein Translocation Across the Endoplasmic Reticulum. II. Isolation and characterization of the Signal Recognition Particle Receptor. J Cell Biol 95, 470-477.
- · Gorodkin, J., Knudsen, B., Zwieb, C., and Samuelsson, T. (2001). SRPDB (Signal Recognition Particle Database). Nucleic Acids Res 29, 169-170.
- · Gowda, K., and Zwieb, C. (1997). Determinants of a protein-induced RNA switch in the large domain of signal recognition particle identified by systematic-site directed mutagenesis. Nucleic Acids Res 25, 2835-2840.
- · Groebe, D. R., and Uhlenbeck, O. C. (1988). Characterization of RNA hairpin loop stability. Nucleic Acids Res 16, 11725-11735.
- · 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 153, 745-762.
- · 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 9, 566-573.
- · Gundelfinger, E. D., Carlo, M. D., Zopf, D., and Melli, M. (1984). Structure and evolution of the 7SL RNA component of the signal recognition particle. Embo J 3, 2325-2332.
- · 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 11, 7363-7374.
- · Hainzl, T., Huang, S., and Sauer-Eriksson, A. E. (2002). Structure of the SRP19 RNA complex and implications for signal recognition particle assembly. Nature 417, 767-771.
- · Hann, B. C., and Walter, P. (1991). The Signal Recognition Particle in S. cerevisiae. Cell 67, 131-144.
- · Hauser, S., Bacher, G., Dobberstein, B., and Lutcke, H. (1995). A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins. Embo J 14, 5485-5493.
- · Hopfield, J. J. (1974). Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity. Proc Natl Acad Sci U S A 71, 4135-4139.
- · Hsu, L. M., Zagorski, J., and Fournier, M. J. (1984). Cloning and sequence analysis of the Escherichia coli 4.5S RNA Gene. Journal of Molecular Biology 178, 509-531.
- · Ibrahimi, I. (1987). Signal recognition particle causes a transient arrest in the biosynthesis of prepromelittin and mediates its translocation across mammalian endoplasmic reticulum. J Cell Biol 104, 61-66.
- · 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 37, 15408-15413.
- · Jagath, J. R., Rodnina, M. V., and Wintermeyer, W. (2000). Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP. Journal of Molecular Biology 295, 745-753.
- · Janiak, F., Walter, P., and Johnson, A. E. (1992). Fluorescence-Detected Assembly of the Signal Recognition Particle: Binding of the Two SRP Protein Heterodimers to SRP RNA Is Non cooperative. Biochemistry 31, 5830-5840.
- · Jensen, C. G., Brown, S., and Pedersen, S. (1994). Effect of 4.5S RNA depletion on Escherichia coli protein synthesis and secretion. J Bacteriol 176, 2502-2506.
- · Johnson, A. E., and van Waes, M. A. (1999). The translocon: a dynamic gateway at the ER membrane. Annu Rev Cell Dev Biol 15, 799-842.
- · Kaine, B. P. (1990). Structure of the Archaebacterial 7S RNA Molecule. Molecular and General Genetics 221, 315-321.
- · Kandels-Lewis, S., and Seraphin, B. (1993). Involvement of U6 snRNA in 5' splice site selection. Science 262, 2035-2039.
- · Keegstra, K., and Cline, K. (1999). Protein import and routing systems of chloroplasts. Plant Cell 11, 557-570.
- · Keenan, R. J., Freymann, D. M., Stroud, R. M., and Walter, P. (2001). The signal recognition particle. Annu Rev Biochemistry 70, 755-775.
- · 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 94, 181-191.
- · 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 146, 55-94.
- · 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 9, 740-744.
- · Kurita, K., Honda, K., Suzuma, S., Takamatsu, H., Nakamura, K., and Yamane, K. (1996). Identification of a region of Bacillus subtilis Ffh, a homologue of mammalian SRP54 protein, that is essential for binding to small cytoplasmic RNA. J Biol Chem 271, 13140-13146.
- · Kurzchalia, T. V., Wiedmann, M., Girshovich, A. S., Bochkareva, E. S., Bielka, H., and Rapoport, T. A. (1986). The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle. Nature 320, 634-636.
- · Ladner, J. E., Jack, A., Robertus, J. D., Brown, R. S., Rhodes, D., Clark, B. F., and Klug, A. (1975). Structure of yeast phenylalanine transfer RNA at 2.5 A resolution. Proc Natl Acad Sci U S A 72, 4414-4418.
- · Larsen, N., and Zwieb, C. (1991). SRP-RNA sequence alignment and secondary structure. Nucleic Acids Res 19, 209-215.
- · 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 275, 27439-27446.
- · Lingelbach, K., Zwieb, C., Webb, J. R., Marshallsay, C., Hoben, P. J., Walter, P., and Dobberstein, B. (1988). Isolation and characterization of a cDNA clone encoding the 19 kDa protein of the signal recognition particle (SRP): expression and binding to 7SL RNA. Nucleic Acids Res 16, 9431-9442.
- · Lipp, J., Dobberstein, B., and Haeuptle, M.-T. (1987). Signal Recognition Particle Arrest Elongation of Nascent Secretory and Membrane Proteins at Multiple Sites in a Transient Manner. J Biol Chem 262, 1680-1684.
- · Liu, L., Ben-Shlomo, H., Xu, Y. X., Stern, M. Z., Goncharov, I., Zhang, Y., and Michaeli, S. (2003). The Trypanosomatid Signal Recognition Particle Consists of Two RNA Molecules, a 7SL RNA Homologue and a Novel tRNA-like Molecule. J Biol Chem 278, 18271-18280.
- · Lu, Y., Qi, H. Y., Hyndman, J. B., Ulbrandt, N. D., Teplyakov, A., Tomasevic, N., and Bernstein, H. D. (2001). Evidence for a novel GTPase priming step in the SRP protein targeting pathway. Embo J 20, 6724-6734.
- · Lütcke, H. (1995). Signal recognition particle (SRP), a ubiquitous initiator of protein translocation. Eur J Biochem 228, 531-550.
- · Lütcke, H., High, S., Römisch, K., Ashford, A. J., and Dobberstein, B. (1992). The menthionine-rich domain of the 54 kDa subunit of signal recognition particle is sufficient for the interaction with signal sequences. Embo J 11, 1543-1551.
- · Lütcke, 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 121, 977-985.
- · Macao, B., Luirink, J., and Samuelsson, T. (1997). Ffh and FtsY in a Mycoplasma mycoides signal-recognition particle pathway: SRP RNA and M domain of Ffh are not required for stimulation of GTPase activity in vitro. Mol Microbiol 24, 523-534.
- · Mason, N., Ciufo, L. F., and Brown, J. D. (2000). Elongation arrest is a physiologically important function of signal recognition particle. Embo J 19, 4164-4174.
- · Matlack, K. E., Mothes, W., and Rapoport, T. A. (1998). Protein translocation: tunnel vision. Cell 92, 381-390.
- · Matlin, K. S. (2002). The strange case of the signal recognition particle. Nature Reviews Molecular Cell Biology 3, 538-542.
- · Menetret, J. F., Neuhof, A., Morgan, D. G., Plath, K., Radermacher, M., Rapoport, T. A., and Akey, C. W. (2000). The structure of ribosome-channel complexes engaged in protein translocation. Mol Cell 6, 1219-1232.
- · Meyer, D. I., and Dobberstein, B. (1980a). Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum. J Cell Biol 87, 503-508.
- · Meyer, D. I., and Dobberstein, B. (1980b). A membrane component essential for vectorial translocation of nascent proteins across the endoplasmic reticulum: requirements for its extraction and reassociation with the membrane. J Cell Biol 87, 498-502.
- · Meyer, D. I., Krause, E., and Dobberstein, B. (1982). Secretory protein translocation across membranes- the role of the docking protein. Nature 297, 647-650.
- · 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 367, 657-659.
- · Miller, J. D., Tajima, S., Lauffer, L., and Walter, P. (1995). The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane. J Cell Biol 128, 273-282.
- · 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 366, 351-354.
- · Millman, J. S., Qi, H. Y., Vulcu, F., Bernstein, H. D., and Andrews, D. W. (2001). FtsY binds to the Escherichia coli inner membrane via interactions with phosphatidylethanolamine and membrane proteins. J Biol Chem 276, 25982-25989.
- · Moazed, D., and Noller, H. F. (1989). Intermediate states in the movement of transfer RNA in the ribosome. Nature 342, 142-148.
- · Montoya, G., Svensson, C., Luirink, J., and Sinning, I. (1997). Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature 385, 365-368.
- · 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 94, 11339-11344.
- · Nakamura, K., Fujii, Y., Shibata, T., and Yamane, K. (1999a). Depletion of Escherichia coli 4.5S RNA leads to an increase in the amount of protein elongation factor EF-G associated with ribosomes. Eur J Biochem 259, 543-550.
- · Nakamura, K., Miyamoto, H., Suzuma, S., Sakamoto, T., Kawai, G., and Yamane, K. (2001). Minimal functional structure of Escherichia coli 4.5 S RNA required for binding to elongation factor G. J Biol Chem 276, 22844-22849.
- · Nakamura, K., Yahagi, S., Yamazaki, T., and Yamane, K. (1999b). 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 274, 13569-13576.
- · 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 245, 720-729.
- · Ninio, J. (1975). Kinetic amplification of enzyme discrimination. Biochimie 57, 587-595.
- · Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Reshetnikova, L., Clark, B. F., and Nyborg, J. (1995). Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science 270, 1464-1472.
- · Noller, H. F., Green, R., Heilek, G., Hoffarth, V., Huttenhofer, A., Joseph, S., Lee, I., Lieberman, K., Mankin, A., Merryman, C., and et al. (1995). Structure and function of ribosomal RNA. Biochem Cell Biol 73, 997-1009.
- · Nyborg, J., Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., and Clark, B. F. (1996). Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation. Trends Biochem Sci 21, 81-82.
- · O'Connor, M., Brunelli, C. A., Firpo, M. A., Gregory, S. T., Lieberman, K. R., Lodmell, J. S., Moine, H., Van Ryk, D. I., and Dahlberg, A. E. (1995). Genetic probes of ribosomal RNA function. Biochem Cell Biol 73, 859-868.
- · 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 81, 1075-1084.
- · Oubridge, C., Kuglstatter, A., Jovine, L., and Nagai, K. (2002). Crystal structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle. Mol Cell 9, 1251-1261.
- · Pakhomova, O. N., Deep, S., Huang, Q., Zwieb, C., and Hinck, A. P. (2002). Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle. Journal of Molecular Biology 317, 145-158.
- · 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 288, 1640-1643.
- · Peluso, P., Shan, S. O., Nock, S., Herschlag, D., and Walter, P. (2001). Role of SRP RNA in the GTPase cycles of Ffh and FtsY. Biochemistry 40, 15224-15233.
- · Pley, H. W., Flaherty, K. M., and McKay, D. B. (1994). Three-dimensional structure of a hammerhead ribozyme. Nature 372, 68-74.
- · Pohlschroder, M., Prinz, W. A., Hartmann, E., and Beckwith, J. (1997). Protein translocation in the three domains of life: variations on a theme. Cell 91, 563-566.
- · Politz, J. C., Lewandowski, L. B., and Pederson, T. (2002). Signal recognition particle RNA localization within the nucleolus differs from the classical sites of ribosome synthesis. J Cell Biol 159, 411-418.
- · 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 97, 55-60.
- · 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 297, 1345-1348.
- · Poritz, M. A., Siegel, V., Hansen, W., and Walter, P. (1988a). Small ribonucleoproteins in Schizosaccharomyces pombe and Yarrowia lipolytica homologous to signal recognition particle. Proc Natl Acad Sci U S A 85, 4315-4319.
- · Poritz, M. A., Strub, K., and Walter, P. (1988b). Human SRP RNA and E. coli 4.5S RNA contain a highly homologous structural domain. Cell 55, 4-6.
- · Powers, T., and Walter, P. (1995). Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases. Science 269, 1422-1424.
- · Prescott, C. D., and Dahlberg, A. E. (1990). A single base change at 726 in 16S rRNA radically alters the pattern of proteins synthesized in vivo. Embo J 9, 289-294.
- · Rapiejko, P., and Gilmore, R. (1992). Protein translocation across the ER requires a functional GTP binding site in the a-subunit of the signal recognition particle receptor. J Cell
- · Biol 117, 493-503.
- · Rapoport, T. A., Heinrich, R., Walter, P., and Schulmeister, T. (1987). Mathematical Modelling of the Effects of the Signal Recognition Particle on Translation and Translocation of Proteins Across the Endoplasmic Reticulum Membrane. Journal of Molecular Biology 195, 621-636.
- · Ribes, V., Romisch, K., Giner, A., Dobberstein, B., and Tollervey, D. (1990). E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle. Cell 63, 591-600.
- · Rinke-Appel, J., Osswald, M., von Knoblauch, K., Mueller, F., Brimacombe, R., Sergiev, P., Avdeeva, O., Bogdanov, A., and Dontsova, O. (2002). Cross linking of 4.5S RNA to the
- · Escherichia coli ribosome in the presence or absence of the protein Ffh. Rna 8, 612-625.
- · Rodnina, M. V., Daviter, T., Gromadski, K., and Wintermeyer, W. (2002). Structural dynamics of ribosomal RNA during decoding on the ribosome. Biochimie 84, 745-754.
- · Rodnina, M. V., Pape, T., Fricke, R., Kuhn, L., and Wintermeyer, W. (1996). Initial binding of the elongation factor Tu.GTP.aminoacyl-tRNA complex preceding codon recognition on the ribosome. J Biol Chem 271, 646-652.
- · Rodnina, M. V., Savelsbergh, A., Katunin, V. I., and Wintermeyer, W. (1997). Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome [see comments]. Nature 385, 37-41.
- · Römisch, 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 111, 1793-1802.
- · Rosenblad, M. A., Gorodkin, J., Knudsen, B., Zwieb, C., and Samuelsson, T. (2003). SRPDB: Signal Recognition Particle Database. Nucleic Acids Res 31, 363-364.
- · Samuelsson, T., and Guindy, Y. (1990). Nucleotide Sequence of a Mycoplasma mycoides RNA which is homologous to E. coli 4.5S RNA. Nucleic Acids Res 18, 4938.
- · Schwartz, T., and Blobel, G. (2003). Structural basis for the function of the Beta subunit of the eukaryotic signal recognition particle receptor. Cell 112, 793-803.
- · Scott, W. G., Finch, J. T., and Klug, A. (1995). The crystal structure of an all-RNA hammerhead ribozyme: a proposed mechanism for RNA catalytic cleavage. Cell 81, 991-1002.
- · Scoulia, E., Krause, E., Meese, K., and Dobberstein, B. (1987). Disassembly and domain structure of the proteins in the signal-recognition particle. Eur J Biochem 163, 519-528.
- · Siegel, V., and Walter, P. (1985). Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane. J Cell Biol 100, 1913-1921.
- · Siegel, V., and Walter, P. (1986). Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact. Nature 320, 81-84.
- · Siegel, V., and Walter, P. (1988a). The affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length. Embo J 7, 1769-1775.
- · Siegel, V., and Walter, P. (1988b). 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 U S A 85, 1801-1805.
- · Siegel, V., and Walter, P. (1988c). Each of the Activities of Signal Recognition Particle (SRP) Is Contained within a Distinct Domain: Analysis of Biochemical Mutants of SRP. Cell 52, 39-49.
- · Siegel, V., and Walter, P. (1988d). Functional dissection of the signal recognition particle. Trends Biochem Sci 13, 314-316.
- · Stark, H., Rodnina, M. V., Rinke Appel, J., Brimacombe, R., Wintermeyer, W., and van Heel, M. (1997). Visualization of elongation factor Tu on the Escherichia coli ribosome. Nature 389, 403-406.
- Stark, H., Rodnina, M. V., Wieden, H. J., Zemlin, F., Wintermeyer, W., and van Heel, M. (2002). Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex. Nat Struct Biol 9, 849-854.
- Strub, K., Fornallaz, M., and Bui, N. (1999). The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure. Rna 5, 1333.
- Strub, K., Moss, J., and Walter, P. (1991). Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution. Mol Cell Biol 11, 3949-3959.
- Strub, K., and Walter, P. (1990). Assembly of the Alu domain of the signal recognition particle (SRP): dimerisation of the two protein components is required for efficient binding to
- SRP RNA. Mol Cell Biol 10, 777-784.
- Struck, J. C. R., Toschka, H. Y., Specht, T., and Erdmann, V. A. (1988). Common structural features between eukaryotic 7SL RNAs, eubacterial 4.5S RNA and scRNA and archaebacterial 7S RNA. Nucleic Acids Res 16, 7740.
- Su, L., Chen, L., Egli, M., Berger, J. M., and Rich, A. (1999). Minor groove RNA triplex in the crystal structure of a ribosomal frameshifting viral pseudoknot. Nat Struct Biol 6, 285-292.
- Suzuma, S., Hayashi, K., Nakamura, K., and Yamane, K. (1999). Analysis of Escherichia coli 4.5S RNA binding affinity to Ffh and EF-G. FEMS Microbiol Lett 180, 271-277.
- Tajima, S., Lauffer, L., Rath, V. L., and Walter, P. (1986). The Signal Recognition Particle Is a complex That Contains Two Distinct Polypeptide chains. J Cell Biol 103, 1167-1178.
- 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 25, 1920-1929.
- Uchiumi, T., Kikuchi, M., Terao, K., Iwasaki, K., and Ogata, K. (1986). Cross-linking of elongation factor 2 to rat-liver ribosomal proteins by 2-iminothiolane. Eur J Biochem 156, 37-48.
- Ullu, E., Murphy, S., and Melli, M. (1982). Human 7SL RNA consists of a 140 nucleotide middle-repetitive sequence inserted in an Alu sequence. Cell 29, 195-202.
- Ullu, E., and Tschudi, C. (1984). Alu sequences are processed 7SL RNA genes. Nature 312, 171-172.
- Utz, P. J., Hottelet, M., Le, T. M., Kim, S. J., Geiger, M. E., van Venrooij, W. J., and Anderson, P. (1998). The 72-kDa component of signal recognition particle is cleaved during apoptosis. J Biol Chem 273, 35362-35370.
- Vila-Sanjurjo, A., and Dahlberg, A. E. (2001). Mutational analysis of the conserved bases C1402 and A1500 in the centre of the decoding domain of Escherichia coli 16 S rRNA reveals an important tertiary interaction. Journal of Molecular Biology 308, 457-463.
- Walter, P., and Blobel, G. (1980). Purification of membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc Natl Acad Sci U S A 77, 7112-7116.
- Walter, P., and Blobel, G. (1981a). Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein. J Cell Biol 91, 551-556.
- Walter, P., and Blobel, G. (1981b). Translocation of proteins across the endoplasmic reticulum. III. Signal recognition protein (SRP) causes signal sequence and site specific arrest of chain elongation that is released by microsomal membranes. J Cell Biol 91, 557-561.
- Walter, P., and Blobel, G. (1983a). Disassembly and Reconstitution of the Signal Recognition Particle. Cell 34, 525-533.
- Walter, P., and Blobel, G. (1983b). Preparation of Microsomal Membranes for Cotranslational Protein Translocation. Methods Enzymol 96, 84-93.
- 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 91, 545-550.
- Weichenrieder, O., Kapp, U., Cusack, S., and Strub, K. (1997). Identification of a minimal Alu RNA folding domain that specifically binds SRP9/14. Rna 3, 1262-1274.
- Weichenrieder, O., Stehlin, C., Kapp, U., Birse, D. E., Timmins, P. A., Strub, K., and Cusack, S. (2001). Hierarchical assembly of the Alu domain of the mammalian signal recognition particle. Rna 7, 731-740.
- Weichenrieder, O., Wild, K., Strub, K., and Cusack, S. (2000). Structure and assembly of the Alu domain of the mammalian signal recognition particle. Nature 408, 167-173.
- Wild, K., Sinning, I., and Cusack, S. (2001). Crystal structure of an early protein-RNA assembly complex of the signal recognition particle. Science 294, 598-601.
- Wilson, K. S., and Noller, H. F. (1998). Molecular movement inside the translational engine. Cell 92, 337-349.
- Wimberly, B. T., Guymon, R., McCutcheon, J. P., White, S. W., and Ramakrishnan, V. (1999). A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Cell 97, 491-502.
- Wolin, S. L., and Walter, P. (1988). Ribosome pausing and stacking during translation of a eukaryotic mRNA. Embo J 7, 3559-3569.
- Wolin, S. L., and Walter, P. (1989). Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate. J Cell Biol 109, 2617-2622.
- 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 116, 605-616.
- Young, J. C., Ursini, J., Legate, K. R., Miller, J. D., Walter, P., and Andrews, D. W. (1995). An amino-terminal domain containing hydrophobic and hydrophilic sequences binds the signal recognition particle receptor alpha subunit to the beta subunit on the endoplasmic reticulum membrane. J Biol Chem 270, 15650-15657.
- Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H., and Noller, H. F. (2001). Crystal structure of the ribosome at 5.5 A resolution. Science 292, 883-896.
- 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 1, 79-87.
- Zopf, D., Bernstein, H. D., and Walter, P. (1993). GTPase domain of the 54kD subunit of the mammalian signal recognition particle is required for protein translocation but not for signal sequence binding. J Cell Biol 120, 1113-1121.
- Zwieb, C. (1992). Recognition of a Tetranucleotide Loop of Signal Recognition Particle RNA by Protein SRP19. J Biol Chem 267, 15650-15656.
- Zwieb, C. (1994). Site-directed mutagenesis of signal-recognition particle RNA. Identification of the nucleotides in helix 8 required for interaction with protein SRP19. Eur J Biochem 222, 885-890.
- Zwieb, C., and Larsen, N. (1997). The Signal Recognition Particle Database (SRPDB). Nucleic Acids Res 25, 107-108.
- Zwieb, C., Muller, F., and Larsen, N. (1996). Comparative analysis of tertiary structure elements in signal recognition particle RNA. Fold Des 1, 315-324.
- Zwieb, C., and Ullu, E. (1986). Identification of dynamic sequences in the central domain of 7SL RNA. Nucleic Acids Res 14, 4639-4657.
[Previous]