Signal recognition particle-dependent targeting of ribosomes to the rough endoplasmic reticulum in the absence and presence of the nascent polypeptide-associated complex

Molecular Biology of the Cell

Volumn 9, Issue 1, 1998, Pages 117-130

  Raden, David ^a   Gilmore, Reid ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATE; MESSENGER RNA; OLIGOMER; POLYPEPTIDE; SIGNAL PEPTIDE; SIGNAL RECOGNITION PARTICLE;

ANIMAL TISSUE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DOG; MEMBRANE BINDING; NONHUMAN; PANCREAS; PRIORITY JOURNAL; RIBOSOME; ROUGH ENDOPLASMIC RETICULUM;

ANIMALIA; CANIS FAMILIARIS; ORYCTOLAGUS CUNICULUS; TRITICUM AESTIVUM;

EID: 0031933791     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.1.117     Document Type: Article

References (45)

1. Adelman, MR., Sabatini, D.D., and Blobel, G. (1973). Ribosome-membrane interaction: nondestructive disassembly of rat liver rough microsomes into ribosomal and membrane components. J. Cell Biol. 56, 206-229.
2. 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. Nature 381, 248-251.
3. Borgese, N., Mok, W., Kreibich, G., and Sabatini, D.D. (1974). Ribosomal-membrane interaction: in vitro binding of ribosomes to microsomal membranes. J. Mol. Biol. 88, 559-580.
4. Connolly, T., Collins, P., and Gilmore, R. (1989). Access of proteinase K to partially translocated nascent polypeptides in intact and detergent-solubilized membranes. J. Cell Biol. 108, 299-307.
5. Connolly, T., and Gilmore, R. (1986). Formation of a functional ribosome-membrane junction during protein translocation requires the participation of a GTP-binding protein. J. Cell Biol. 103, 2253-2261.
6. 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.
7. 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.
8. Crowley, K.S., Liao, S., Worrell, V.E., Reinhart, G.D., and Johnson, A.E. (1994). Secretory proteins move through the endoplasmic reticulum via an aqueous, gated pore. Cell 78, 461-471.
9. Gilmore, R., and Blobel, G. (1985). Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants. Cell 42, 497-505.
10. Gilmore, R., Collins, P., Johnson, J., Kellaris, K., and 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.
11. Görlich, D., Prehn, S., Hartmann, E., Kalies, K.-U., and Rapoport, T.A. (1992). A mammalian homologue of Sec61p and SecYp is associated with ribosomes and nascent polypeptides during translocation. Cell 71, 489-503.
12. Görlich, D., and Rapoport, T.A. (1993). Protein translocation into proteoliposomes reconstituted from purified components of the ER membrane. Cell 75, 615-630.
13. Hanein, D., Matlack, K.E.S., Jungnickel, B., Plath, K., Kalies, K.-U., Miller, K.R., Rapoport, T.A., and Akey, C.W. (1996). Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Cell 87, 721-732.
14. Jackson, R.J., and Hunt, T. (1983). Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA. Methods Enzymol. 96, 50-74.
15. Jungnickel, B., and Rapoport, T.A. (1995). A posttranslational signal sequence recognition event in the endoplasmic reticulum membrane. Cell 82, 261-270.
16. Kalies, K.-U., Görlich, D., and Rapoport, T.A. (1994). Binding of ribosomes to the rough endoplasmic reticulum is mediated by the Sec61p-complex. J. Cell Biol. 126, 925-934.
17. Kellaris, K.V., Bowen, S., and Gilmore, R. (1991). Endoplasmic reticulum translocation intermediates are adjacent to a non-glycosylated 34 kD integral membrane protein. J. Cell Biol. 114, 21-33.
18. Krieg, U.C., Walter, P., and Johnson, A.E. (1986). Photocrosslinking of the signal sequence of nascent preprolactin to the 54 kD polypeptide of the signal recognition particle. Proc. Natl. Acad. Sci. USA 83, 8604-8608.
19. 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 54 kD polypeptide of the signal recognition particle. Nature 320, 634-636.
20. Lauring, B., Kreibich, G., and Wiedmann, M. (1995a). The intrinsic ability of ribosomes to bind to endoplasmic reticulum membranes is regulated by signal recognition particle and nascent polypeptide-associated complex. Proc. Natl. Acad. Sci. USA 92, 9435-9439.
21. Lauring, B., Sakai, H., Kreibich, G., and Wiedmann, M. (1995b). Nascent polypeptide-associated complex protein prevents mistar-geting of nascent chains to the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 92, 5411-5415.
22. Meyer, D.I., Krause, E., and Dobberstein, B. (1982). Secretory protein translocation across membranes: the role of the 'docking protein'. Nature 297, 647-650.
23. Miller, J.D., Wilhelm, H., Gierasch, R., Gilmore, R., and Walter, P. (1993). GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature 366, 351-354.
24. Muller, G., and Zimmermann, R. (1987). Import of honeybee pre-promelittin into the endoplasmic reticulum: structural basis for independence of SRP and docking protein. EMBO J. 6, 2099-2107.
25. Murphy, E.C.I., Zheng, T., and Nicchitta, C.V. (1997). Identification of a novel stage of ribosome/nascent chain association with the endoplasmic reticulum. J. Cell Biol. 136, 1213-1226.
26. Nicchitta, C.V., Murphy, E.C.I., Haynes, R., and Shelness, G.S. (1995). Stage- and ribosome-specific alterations in nascent chain-Sec61p interactions accompany translocation across the ER membrane. J. Cell Biol. 229, 957-970.
27. Perara, E., Rothman, R.E., and Lingappa, V.R. (1986). Uncoupling translocation from translation: implications for transport of proteins across membranes. Science 232, 348-352.
28. Powers, T., and Walter, P. (1996). The nascent polypeptide-associated complex modulates interactions between the signal recognition particle and the ribosome. Current Biol. 6, 331-338.
29. Rapiejko, P.J., 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.
30. Rapiejko, P.J., and 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.
31. Rapiejko, P.J., and Gilmore, R. (1997). Empty site forms of the SRP54 and SRα GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum. Cell 89, 703-713.
32. Sabatini, D.D., Tashiro, Y., and Palade, G.E. (1966). On the attachment of ribosomes to microsomal membranes. J. Mol. Biol. 19, 503-524.
33. Schägger, H., and von Jagow, G. (1987). Tricine-sodium dodecyl-sulphate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1-100 kDa. Anal. Biochem. 166, 368-379.
34. Schlenstedt, G., and Zimmermann, R. (1987). Import of frog pre-propeptide GLa into microsomes requires ATP but does not involve docking protein or ribosomes. EMBO J. 6, 699-703.
35. 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.
36. Simon, S.M., and Blobel, G. (1991). A protein-conducting channel in the endoplasmic reticulum. Cell 65, 371-380.
37. Tashiro, Y., and Siekevitz, P. (1965). Ultracentrifugal studies on the dissociation of hepatic ribosomes. J. Mol. Biol. 11, 149-165.
38. 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. 92, 551-556.
39. Walter, P., and Blobel, G. (1981b). 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.
40. Walter, P., and Blobel, G. (1983). Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 96, 84-93.
41. 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.
42. Walter, P., and Johnson, A.E. (1994). Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10, 87-119.
43. Wang, S., Sakai, H., and Wiedmann, M. (1995). NAC covers ribosome-associated nascent chains thereby forming a protective envi- ronment for regions of nascent chains just emerging from the peptidyl transferase center. J. Cell Biol. 130, 519-528.
44. Wickner, W. (1995). The nascent-polypeptide-associated complex: having a "NAC" for fidelity of translation. Proc. Natl. Acad. Sci. USA 92, 9433-9434.
45. Wiedmann, B., Sakai, H., Davis, T.A., and Wiedmann, M. (1994). A protein complex required for signal-sequence-specific sorting and translocation. Nature 370, 434-440.