The N-domain of the signal recognition particle 54-kDa subunit promotes efficient signal sequence binding

European Journal of Biochemistry

Volumn 245, Issue 3, 1997, Pages 720-729

  Newitt, John A ^a   Bernstein, Harris D ^a,b  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

endoplasmic reticulum; GTP; ribonucleoprotein; signal; signal recognition particle

Indexed keywords

GUANOSINE TRIPHOSPHATE; RIBONUCLEOPROTEIN; SIGNAL RECOGNITION PARTICLE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; ENDOPLASMIC RETICULUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN RNA BINDING; SIGNAL TRANSDUCTION;

ANIMALIA;

EID: 0030907638     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00720.x     Document Type: Article

References (49)

1. Walter, P. & Johnson, A. E. (1994) Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane, Annu. Rev. Cell Biol. 10, 87-119.
2. Walter, P. & 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. 91, 557-561.
3. Miller, J. D., Tajima, S., Lauffer, L. & Walter, P. (1995) The β subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the α subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane, J. Cell Biol. 128, 273-282.
4. Connolly, T. & 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.
5. Gilmore, R., Walter, P. & Blobel, G. (1982) Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor, J. Cell Biol. 95, 470-477.
6. Meyer, D. I., Krause, E. & Dobberstein, B. (1982) Secretory protein translocation across membranes-the role of the 'docking protein', Nature 297, 647-650.
7. Tajima, S., Lauffer, L., Rath, V. L. & Walter, P. (1986) The signal recognition particle receptor is a complex that contains two distinct polypeptide chains, J. Cell Biol. 103, 1167-1178.
8. Görlich, D., Hartmann, R., Prehn, S. & Rapoport, T. A. (1992) A protein of the endoplasmic reticulum involved early in polypeptide translocation, Nuture 357, 47-52.
9. Görlich, D. & Rapoport, T. A. (1993) Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane, Cell 75, 615-630.
10. Gilmore, R., Blobel, G. & 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. 95, 463-469.
11. Schatz, G. & Dobberstein, B. (1996) Common principles of protein translocation across membranes, Science 271, 1519-1526.
12. Kurzchalia, T. V., Wiedmann, M., Girshovich, A. S., Bochkareva, H. S., Bielka, H. & Rapoport, T. A. (1986) The signal sequence of nascent preprolactin interacts with the 54 K polypeptide of the signal recognition particle, Nature 320, 634-636.
13. Krieg, U. C., Walter, P. & Johnson, A. E. (1986) Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle, Proc. Natl Acad. Sci. USA 83, 8604-8608.
14. Siegel, V. & 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 52, 39-49.
15. Römisch, K., Webb, J., Lingelbach, K., Gausepohl, H. & Dobberstein, B. (1990) The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain, J. Cell Biol. 111, 1793-1802.
16. Zopf, D., Bernstein, H. D., Johnson, A. E. & 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. 9, 4511-4517.
17. Zopf, D., Bernstein, H. D. & 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. 120, 1113-1121.
18. Lütcke, H., High, S., Römisch, K., Ashford, A. J. & Dobberstein, B. (1992) The methionine-rich domain of the 54 kDa subunit of signal recognition particle is sufficient for the interaction with signal sequences, EMBO J. 11, 1543-1551.
19. Bernstein, H. D., Poritz, M. A., Strub, K., Hoben, P. J., Brenner, S. & Walter, P. ( 1989) Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle, Nature 340, 482-486.
20. Römisch, K., Webb, J., Herz, J., Prehn, S., Frank, R., Vingron, M. & Dobberstein, B. (1989) Homology of 54 K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains, Nature 340, 478-482.
21. Powers, T. & Walter, P. (1995) Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases, Science 269, 1422-1424.
22. Freymann, D. M., Keenan, R. J., Stroud, R. M. & Walter, P. (1997) Structure of the conserved GTPase domain of the signal recognition particle, Nature 385, 361-364.
23. Bacher, G., Lütcke, H., Jungnickel, B., Rapoport, T. & Dobberstein, B. (1996) Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting, Nature 381, 248-251.
24. Bourne, H. R., Sanders, D. A. & McCormick, F. (1991) The GTPase superfamily: conserved structure and molecular mechanism, Nature 349, 117-127.
25. Hansen, W., Garcia, P. D. & Walter, P. (1986) In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent posttranslational translocation of the prepro-alpha-factor. Cell 45, 397-406.
26. Sarkar, G. & Sommer, S. S. (1990) The 'megaprimer' method of site-directed mutagenesis, Biotechniques 8, 404-407.
27. Siegel, V. & Walter, P. (1985) Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane, J. Cell Biol. 100, 1913-1921.
28. Walter, P. & Blobel, G. (1983) Preparation of microsomal membranes for cotranslational protein translocation, Methods Enzymol. 96, 84-93.
29. Walter, P. & Blobel, G. (1983) Disassembly and reconstitution of signal recognition particle, Cell 34, 525-533.
30. Chang, D.-Y., Newitt, J. A., Hsu, K., Bernstein, H. D. & 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, 1117-1123.
31. Webb, N. R. & Summers, M. D. (1990) Expression of proteins using recombinant baculoviruses, Technique 2, 173-188.
32. O'Reilly, D. R., Miller, L. K. & Luckow, V. A. (1992) Baculovirus expression vectors: a laboratory manual, W. H. Freeman and Co., NY.
33. Strub, K. & 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. 10, 777-784.
34. Gilmore, R., Collins, P., Johnson, J., Kellaris, K. & Rapiejko, P. (1991) Transcription of full-length and truncated mRNA transcripts to study protein translocation across the endoplasmic reticulum, Methods Cell Biol. 34, 223-239.
35. Bos, J. L., Toksoz, D., Marshall, C. J., Verlann-de Vries, M., Veeneman, G. H., van der Eb, A. J., van Boom, J. H., Janssen, J. W. G. & Steenvoorden, A. C. M. (1985) Amino-acid substitutions at codon 13 of the N-ras oncogene in human acute myeloid leukaemia, Nature 315, 726-730.
36. Polakis, P. & McCormick, F. (1993) Structural requirements for the interaction of p21ras with GAP, exchange factors, and its biological effector target, J. Biol. Chem. 268, 9157-9160.
37. Miller, R. T., Masters, S. B., Sullivan, K. A., Beiderman, B. & Bourne, H. R. (1988) A mutation that prevents GTP-dependent activation of the α chain of G, Nature 334, 712-715.
38. Hwang, Y. W., Jurnak, F. & Miller, D. L. (1989) A mutation that hinders GTP induced aminoacyl-tRNA binding of elongation factor Tu, in The guanine-nucleotide binding proteins: common structural and functional properties (Bosch, L., Kraal, B. & Parmeggiani, A., eds) pp. 77-85, Plenum Press, NY.
39. Rapiejko, P. J. & Gilmore, R. (1992) Protein translocation across the ER requires a functional GTP binding site in the α subunit of the signal recognition particle receptor, J. Cell Biol. 117, 493-503.
40. Cordell, B., Bell, G., Tischer, E., DeNoto, F. M., Ullrich, A., Pictet, R., Rutter, W. J. & Goodman, H. M. (1979) Isolation and characterization of a cloned rat insulin gene, Cell 18, 533-543.
41. Lomedico, P., Rosenthal, N., Efstratiadis, A., Gilbert, W., Kolodner, R. & Tizard, R. (1979) The structure and evolution of the two nonallelic rat preproinsulin genes, Cell 18, 545-558.
42. Gussow, D., Rein, R., Ginjaar, I., Hochstenbach, F., Seemann, G., Kottman, A. & Ploegh, H. L. (1987) The human β2-microglobulin gene. Primary structure and definition of the transcriptional unit, J. Immunol. 139, 3132-3138.
43. Connolly, T. & Gilmore, R. (1986) Formation of a functional ribosome-membrane junction during translocation requires the participation of GTP binding, J. Cell Biol. 103, 2253-2261.
44. Siegel, V. & Walter, P. (1986) Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact, Nature 320, 81-84.
45. Ogg, S. C. & 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.
46. Miller, J. D., Wilhelm, H., Gierasch, L., Gilmore, R. & Walter, P. (1993) GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation, Nature 366, 351-354.
47. Rapiejko, P. J. & Gilmore, R. (1994) Signal sequence recognition and targeting of ribosomes to the endoplasmic reticulum by the signal recognition particle do not require GTP, Mol. Biol. Cell 5, 887-897.
48. Berchtold, H., Reshetnikova, L., Reiser, C. O., Schirmer, N. K., Sprinzl, M. & Hilgenfeld, R. (1993) Crystal structure of active elongation factor Tu reveals major domain rearrangements, Nature 365, 126-132.
49. Randazzo, P. A., Terui, T., Sturch, S., Fales, H. M., Ferrige, A. G. & Kahn, R. A. (1995) The myristoylated amino terminus of ADP-ribosylation factor 1 is a phospholipid- and GTP-sensitive switch, J. Biol. Chem. 270, 14 809-14 815.