Elongation arrest is a physiologically important function of signal recognition particle

EMBO Journal

Volumn 19, Issue 15, 2000, Pages 4164-4174

  Mason, Nicola ^a   Ciufo, Leonora F ^a   Brown, Jeremy D ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

Elongation arrest; SRP; Targeting; Translation; Yeast

Indexed keywords

PROTEIN SUBUNIT; SIGNAL RECOGNITION PARTICLE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; GENE TRANSLOCATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; RIBOSOME; TEMPERATURE SENSITIVITY; YEAST;

EUKARYOTA; FUNGI; MAMMALIA; SACCHAROMYCES CEREVISIAE;

EID: 0034254190     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.15.4164     Document Type: Article

References (41)

1. Andrews, D.W., Walter, P. and Ottensmeyer, F.P. (1985) Structure of the signal recognition particle by electron microscopy. Proc. Natl Acad. Sci. USA, 82, 785-789.
2. Birse, D.E.A., Kapp, U., Strüb, 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.
3. 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.
4. Bui, N. and Strüb, K. (1999) New insights into signal recognition and elongation arrest activities of the signal recognition particle. Biol. Chem., 380, 135-145.
5. 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.
6. Felici, F., Cesareni, G. and Hughes, J.M.X. (1989) The most abundant small cytoplasmic RNA of Saccharomyces cerevisiae has an important function required for normal cell growth. Mol. Cell. Biol., 9, 3260-3268.
7. Hann, B.C. and Walter, P. (1991) The signal recognition particle in S.cerevisiae. Cell. 67, 131-144.
8. Hann, B., Stirling, C.J. and Walter, P. (1992) SEC65 gene product is a subunit of the yeast signal recognition particle required for its integrity. Nature, 356, 532-533.
9. Hansen, W. and Walter, P. (1988) Prepro-carboxypeptidase Y and a truncated form of pre-invertase, but not full-length pre-invertase, can be posttranslationally translocated across microsomal vesicle membranes from Saccharomyces cerevisiae. J. Cell Biol., 106, 1075-1081.
10. Hansen, W., Garcia, P.D. and Walter, P. (1986) In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent post-translational translocation of the prepro-α factor. Cell. 45, 397-406.
11. Hauser, S., Bacher, G., Dobberstein, B. and Lütcke, H. (1995) A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins. EMBO J., 14, 5485-5493.
12. Johnsson, N. and Varshavsky, A. (1994) Ubiquitin-assisted dissection of protein transport across membranes. EMBO J., 13, 2686-2698.
13. Krieg, U.C., Walter, P. and 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. 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.
15. Liao, X., Selinger, D., Althoff, S., Chiang, A., Hamilton, D., Ma, M. and Wise, J.A. (1992) Random mutagenesis of Schizosaccharomyces pombe SRP RNA: lethal and conditional lesions cluster in presumptive protein binding sites. Nucleic Acids Res., 20, 1607-1615.
16. Luirink, J., High, S., Wood, H., Giner, A., Tollervey, D. and Dobberstein, B. (1992) Signal sequence recognition by an Escherichia coli ribonucleoprotein complex. Nature, 359, 741-743.
17. Lütcke, H. (1995) Signal recognition particle (SRP), a ubiquitous initiator of protein translocation. Eur. J. Biochem., 228, 531-550.
18. Ng, D.T. and Walter, P. (1996) ER membrane protein complex required for nuclear fusion. J. Cell Biol., 132, 499-509.
19. Ng, D.T.W., Brown, J.D. and Walter, P. (1996) Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J. Cell Biol., 134, 269-278.
20. Ngsee, J.K. and Smith, M. (1990) Changes in a mammalian signal sequence required for efficient protein secretion by yeasts. Gene, 86, 251-255.
21. 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 in translation elongation. Cell, 81, 1075-1084.
22. Ogg, S., Poritz, M. and Walter, P. (1992) The signal recognition particle receptor is important for growth and protein secretion in Saccharomyces cerevisiae. Mol. Biol. Cell, 3, 895-911.
23. Powers, T. and Walter, P. (1996) The nascent polypeptide-associated complex modulates interactions between the signal recognition particle and the ribosome. Curr. Biol., 6, 331-338.
24. Rothe, C. and Lehle, L. (1998) Sorting of invertase signal peptide mutants in yeast dependent and independent on the signal-recognition particle. Eur. J. Biochem., 252, 16-24.
25. 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.
26. 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.
27. 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.
28. Siegel, V. and Walter, P. (1988b) 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.
29. Sikorski, R.S. and Heiter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
30. Stirling, C.J. and Hewitt, E.W. (1992) The Saccharomyces cerevisiae SEC65 gene encodes a component of the yeast signal recognition particle with homology to human SRP19. Nature, 356, 534-537.
31. Stirling, C.J., Rothblatt, J., Hosobuchi, M., Deshaies, R. and Schekman, R. (1992) Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell, 3, 129-142.
32. Strüb, 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.
33. Strüb, 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, 1333-1347.
34. Thomas, Y., Bui, N. and Strüb, 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.
35. Valent, Q.A., Kendall, D.A., High, S., Kusters, R., Oudega, B. and Luirink, J. (1995) Early events in preprotein recognition in E.coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J., 14, 5494-5505.
36. Walter, P. and Blobel, G. (1980) Purification of membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc. Natl Acad. Sci. USA, 77, 7112-7116.
37. Walter, P. and Blobel, G. (1981) 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.
38. 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.
39. Wilkinson, B.M., Tyson, J.R., Reid, P.J. and Stirling, C.J. (2000) Distinct domains within yeast Sec61p involved in post-translational translocation and protein dislocation. J. Biol. Chem., 275, 521-529.
40. 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.
41. Zwieb, C., Muller, F. and Larsen, N. (1996) Comparative analysis of tertiary structure elements in signal recognition particle RNA. Fold. Des., 1, 315-324.