The Srp40 protein plays a dose-sensitive role in preribosome assembly or transport and depends on its carboxy-terminal domain for proper localization to the yeast nucleoskeleton

DNA and Cell Biology

Volumn 16, Issue 10, 1997, Pages 1161-1173

  Ikonomova, Raina ^a,c   Sommer, Thomas ^b   Képès, Francois ^a  

^a CEA SACLAY   (France)

^b MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^c ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; NUCLEOLIN; RIBOSOME PROTEIN; RIBOSOME RNA; SIGNAL RECOGNITION PARTICLE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL NUCLEUS; CELLULAR DISTRIBUTION; CYTOSKELETON; ENDOPLASMIC RETICULUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN TRANSPORT; RIBOSOME; RNA SYNTHESIS; RNA TRANSCRIPTION; YEAST;

MAMMALIA;

EID: 0030726248     PISSN: 10445498     EISSN: None     Source Type: Journal    
DOI: 10.1089/dna.1997.16.1161     Document Type: Article

References (45)

1. BONNEAUD, N., OZIER-KALOGEROPOULOS, O., LI, G., LABOUESSE, M., MINIVIELLE-SEBASTIA, L., and LACROUTE, F. (1991). A family of low and high copy replicative, intcgrative and single-stranded S. cerevisiae/E. coli shuttle vectors. Yeast 7, 609-615.
2. BORER, R.A., LEHNER, C.F., EPPENBERGER, H.M., and NIGG, E.A. (1989). Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell 56, 379-390.
3. CHAUSSIVERT, N. (1995). Rôle de la sous-unité de 131 kDa dans l'architecture et le fonctionnement du facteur de transcription TFIIIC de la levure S. cerevisiae. Louis Pasteur Strasbourg I.
4. CULLIN, C., and MINIVIELLE-SEBASTIA, L. (1994). Multipurpose vectors designed for the fast generation of N- or C-terminal epitope-tagged proteins. Yeast 10, 105-112.
5. DAVIS, L.I., and FINK, G.R. (1990). The NUP1 gene encodes an essential component of the yeast nuclear pore complex. Cell 61, 965-978.
6. DESHAIES, R.J., and SCHEKMAN, R. (1987). A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J. Cell Biol. 105, 633-645.
7. DESSEN, P., FONDRAT, C., VALENCIEN, C., and MUGNIER, C. (1990). BISANCE: A French service for access to biomolecular sequence databases. Comp. Appl. Biosci. 6, 355-356.
8. DONZEAU, M., FANTINO, E., and LAUQUIN, G. (1993). Famille multigénique SRP (serine-rich proteins). Induction par le froid et l'anaérobiose. In: La levure: modèle et outil II Abstract 88.
9. DUJON, B., ALEXANDRAKI, D., ANDRE, B., ANSORGE, W., et al. (1994). Complete DNA sequence of yeast chromosome XI. Nature 369, 371-378.
10. ESNAULT, Y., BLONDEL, M.-O., DESHAIES, R.J., SCHEKMAN, R., and KÉPÈS, F. (1993). The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum. EMBO J. 12, 4083-4093.
11. ESNAULT, Y., FELDHEIM, D., BLONDEL, M.-O., SCHEKMAN, R., and KÉPÈS, F. (1994). SSS1 encodes a stabilizing component of the Secol subcomplex of the yeast protein translocation apparatus. J. Biol. Chem. 269, 27478-27485.
12. ESPINET, C., DE LA TORRE, M.A., ALDEA, M., and HERRERO, E. (1995). An efficient method to isolate yeast genes causing over-expression-mediated growth arrest. Yeast 11, 25-32.
13. FORBES, D.J. (1992). Structure and function of the nuclear pore complex. Annu. Rev. Cell Biol. 8, 495-527.
14. GILSON, E., LAROCHE, T., and GASSER, S.M. (1993). Telomeres and the functional architecture of the nucleus. Trends Cell Biol. 3, 128-134.
15. GOLDBERG, M.W., and ALLEN, T.D. (1993). The nuclear pore complex: three-dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlying structure uncovered by proteolysis. J. Cell Sci. 106, 261-274.
16. HEINE, M.A., RANKIN, M.L., and DiMARIO, P.J. (1993). The Gly/Arg-rich (GAR) domain of Xenopus nucleolin facilitates in vitro nucleic acid binding and in vivo nucleolar localization. Mol. Biol. Cell 4, 1189-1204.
17. ITO, H., FUKUDA, Y., MURATA, K., and KUMURA, A. (1983). Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168.
18. KOWALSKI, L.R., KONDO, K., and INOUYE, M. (1995). Cold-shock induction of a family of TIPl-related proteins associated with the membrane in Saccharomyces cerevisiae. Mol. Microbiol. 15, 341-353.
19. LALO, D., CARLES, C., SENTENAC, A., and THURIAUX, P. (1993). Interactions between three common subunits of yeast RNA polymerases I and III. Proc. Natl. Acad. Sci. USA 90, 5524-5528.
20. LEE, W.-C., XUE, Z., and MÉLÈSE, T. (1991). The NSR1 gene en-codes a protein that specifically binds nuclear localization sequences and has two RNA recognition motifs. J. Cell Biol. 113, 1-12.
21. LEFEBVRE, O., RUTH, J., and SENTENAC, A. (1993). A mutation in the largest subunit of yeast TFIHOC affects tRNA and 5S RNA synthesis. J. Biol. Chem. 269, 23374-23381.
22. MARCK, C. (1988). "DNA Strider": A "C" program for the fast analysis of DNA and protein sequences on the Apple Macintosh family of computers. Nucleic Acids Res. 16, 1829-1836.
23. MEIER, U.T. (1996). Comparison of the Rat nucleolar protein Nopp140 with its yeast homolog SRP40. J. Biol. Chem. 271, 19376-19384.
24. MEIER, U.T., and BLOBEL, G. (1992). Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell 70, 127-138.
25. MIRZAYAN, C., COPELAND, C.S., and SNYDER, M. (1992). The NUF1 gene encodes an essential coiled-coil related protein that is a potential component of the yeast nucleoskeleton. J. Cell Biol. 116, 1319-1332.
26. NASMYTH, K.A., and TATCHELL, K. (1980). The structure of transposable yeast mating type. Cell 19, 753-764.
27. NEHRBASS, U., KERN, H., MUTVEI, A., HORSTMANN, B., MARSHALLSAY, B., and HURT, E.C. (1990). NSP1: A yeast nuclear envelope protein localized at the nuclear pores exerts its essential function by its carboxy-terminal domain. Cell 61, 979-989.
28. OSBORNE, M.A., and SILVER, P.A. (1993). Nucleocytoplasmic transport in the yeast Saccharomyces cerevisiae. Annu. Rev. Biochem. 62, 219-254.
29. PANZNER, S., DREIER, L., HARTMANN, E., KOSTKA, S., and RAPOPORT, T.A. (1995). Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81, 561-570.
30. PHILIPPSEN, P., THOMAS, M., CRAMER, R.A., and DAVIS, R.W. (1978). Unique arrangement of coding sequences for 5S, 5.8S, 18S and 25S ribosomal RNA in Saccharomyces cerevisiae as determined by R loop and hybridization analysis. J. Mol. Biol. 123, 387-404.
31. PRINGLE, J.R., ADAMS, A.E.M., DRUBIN, D.G., and HAARER, B.K. (1991). Immunofluorescence methods for yeast. In Guide to Yeast Genetics and Molecular Biology, vol. 194. C. Guthrie and G.R. Fink, eds. (Academic Press, New York), pp. 565-602.
32. ROSE, M.D., WINSTON, F., and HIETER, P. (1990). Methods in Yeast Genetics. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY).
33. ROTHSTEIN, R. (1983). One-step gene disruption in yeast. Methods Enzymol. 101, 202-211.
34. ROTHSTEIN, R., and THOMAS, B.J. (1989). Elevated recombination rates in transcriptionally active DNA. Cell 56, 619-630.
35. ROUT, M.P., and BLOBEL, G. (1993). Isolation of the yeast nuclear pore complex. J. Cell Biol. 123, 771-783.
36. SAMBROOK, J., FRITSCH, E.F., and MANIATIS, T. (1989). Molecular Cloning: A Laboratory Manual. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY).
37. 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.
38. THURIAUX, P., and SENTENAC, A. (1992). Yeast nuclear RNA polymerases. In The Molecular and Cellular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression, vol. 2. J.N. Strathem, E.W. Jones, and J.K. Broach, eds. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY).
39. URSIC, D., DEMARINI, D.J., and CULBERTSON, M.R. (1995). Inactivation of the yeast Sen1 protein affects the localization of nucleolar proteins. Mol. Gen. Genet. 249, 571-584.
40. VIGNAIS, M.-L., WOUDT, L.P., WASSENAAR, G.M., MAGER, W.H., SENTENAC, A., and PLANTA, R.J. (1987). Specific binding of TUF factor to upstream activation sites of yeast ribosomal protein genes. EMBO J. 6, 1451-1457.
41. VIGNAIS, M.-L., HUET, J., BÜHLER, J.-M., and SENTENAC, A. (1990). Contacts between the factor TUF and RPG sequences. J. Biol. Chem. 265, 14669-14674.
42. WARNER, J.R. (1982). The yeast ribosome: Structure, function, and synthesis. In The Molecular Biology of the yeast Saccharomyces: Metabolism and Gene Expression. J.N. Strathem, E.W. Jones, and J.R. Broach, eds. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY) pp. 529-560.
43. WARNER, J.R. (1991). Labeling of RNA and phosphoproteins in Saccharomyces cerevisiae. Methods of Enzymol. 194, 423-428.
44. XUE, Z., and MÉLÈSE, T. (1994). Nucleolar proteins that bind NLSs: A role in nuclear import or ribosome biogenesis? Trends Cell Biol. 4, 414-417.
45. YANISCH-PERRON, C., VIEIRA, J., and MESSING, J. (1985). Improved M13 phage cloning vectors and host strains: nucleotide sequence of the M13mp18 and pUC19 vectors. Gene 33, 103-110.