A link between secretion and pre-mRNA processing defects in Saccharomyces cerevisiae and the identification of a novel splicing gene, RSE1

Molecular and Cellular Biology

Volumn 18, Issue 12, 1998, Pages 7139-7146

  Chen, Esther J ^a   Frand, Alison R ^a   Chitouras, Elizabeth ^a   Kaiser, Chris A ^a,b  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b Department of Biology ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA FRUCTOFURANOSIDASE; MESSENGER RNA; PROTEINASE;

ARTICLE; ENDOPLASMIC RETICULUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN SECRETION; PROTEIN TRANSPORT; RNA SPLICING; SACCHAROMYCES CEREVISIAE; TEMPERATURE SENSITIVE MUTANT;

EUKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 0031753250     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.12.7139     Document Type: Article

References (42)

1. Adams, A., D. Gottschling, and C. Kaiser. 1996. Methods in yeast genetics: a laboratory course manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
2. Chitouras, E., and C. A. Kaiser. Unpublished data.
3. Church, G. M., and W. Gilbert. 1984. Genomic sequencing. Proc. Natl. Acad. Sci. USA 81:1991-1995.
4. Forrester, W., F. Stutz, M. Rosbash, and M. Wickens. 1992. Defects in mRNA 3′ end formation, transcription initiation, and mRNA transport associated with the yeast mutation prp20: possible coupling of mRNA processing and chromatin structure. Genes Dev. 6:1914-1926.
5. Fromont-Racine, M., J.-C. Rain, and P. Legrain. 1997. Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nat. Genet. 16:277-282.
6. Gimeno, R. E., P. Espenshade, and C. A. Kaiser. 1995. SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation. J. Cell Biol. 131:325-338.
7. Goldstein, A., and J. O. Lampen. 1975. β-D-Fructofuranoside fructohydrolase from yeast. Methods Enzymol. 42:504-511.
8. Gunderson, S. I., K. Beyer, G. Martin, W. Keller, W. C. Boelens, and I. W. Mattaj. 1994. The human U1A snRNP protein regulates polyadenylation via a direct interaction with poly(A) polymerase. Cell 76:531-541.
9. Hartwell, L. H., C. S. McLaughlin, and J. R. Warner. 1970. Identification of ten genes that control ribosome formation in yeast. Mol. Gen. Genet. 109: 42-56.
10. Hartwell, L. H., R. K. Mortimer, J. Culotti, and M. Culotti. 1973. Genetic control of the cell division cycle in yeast. V. Genetic analysis of cdc mutants. Genetics 74:267-286.
11. Hwang, B. J., and G. Chu. 1993. Purification and characterization of a human protein that binds to damaged DNA. Biochemistry 32:1657-1666.
12. Jenny, A., and W. Keller. 1995. Cloning of cDNAs encoding the 160 kDa subunit of the bovine cleavage and polyadenylation specificity factor. Nucleic Acids Res. 23:2629-2635.
13. Kao, H.-Y., and P. G. Siliciano. 1996. Identification of Prp40, a novel essential yeast splicing factor associated with the U1 small nuclear ribonucleoprotein particle. Mol. Cell. Biol. 16:960-967.
14. Kim, S.-H., J. Smith, A. Claude, and R.-J. Lin. 1992. The purified yeast pre-mRNA splicing factor PRP2 is an RNA-dependent NTPase. EMBO J. 11:2319-2326.
15. Krishnamoorthy, R. R., T. H. Lee, J. S. Butel, and H. K. Das. 1997. Apolipoprotein B gene regulatory factor-2 (BRF-2) is structurally and immunologically highly related to hepatitis B virus X associated protein (XAP-1). Biochemistry 36:960-969.
16. Lee, T. H., S. J. Elledge, and J. S. Butel. 1995. Hepatitis B virus X protein interacts with a probable cellular DNA repair protein. J. Virol. 69:1107-1114.
17. Legrain, P., and M. Rosbash. 1989. Some cis- and trans-acting mutants for splicing target pre-mRNA to the cytoplasm. Cell 57:573-583.
18. Liao, X. C., J. Tang, and M. Rosbash. 1993. An enhancer screen identifies a gene that encodes the yeast U1 snRNP A protein: implications for snRNP protein function in pre-mRNA splicing. Genes Dev. 7:419-428.
19. Lin, R.-J., A. J. Lustig, and J. Abelson. 1987. Splicing of yeast nuclear pre-mRNA in vitro requires a functional 40S spliceosome and several extrinsic factors. Genes Dev. 1:7-18.
20. Lutz, C. S., K. G. K. Murthy, N. Schek, J. P. O'Connor, J. L. Manley, and J. C. Alwine. 1996. Interaction between the U1 snRNP-A protein and the 160 kD subunit of cleavage-polyadenylation specificity factor increases polyadenylation in vitro. Genes Dev. 10:325-337.
21. Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
22. Mizuta, K., and J. R. Warner. 1994. Continued functioning of the secretory. pathway is essential for ribosome synthesis. Mol. Cell. Biol. 14:2493-2502.
23. Murthy, K. G., and J. L. Manley. 1995. The 160 kD subunit of human cleavage and polyadenylation specificity factor coordinates pre-mRNA 3′-end formation. Genes Dev. 9:2672-2683.
24. Nakano, A., and M. Muramatsu. 1989. A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Biol. 109:2677-2691.
25. 3H]mannose suicide selection. J. Cell Biol. 105:1587-1594.
26. Niwa, M., and S. M. Berget. 1991. Mutation of the AAUAAA polyadenylation signal depresses in vitro splicing of proximal but not distal introns. Genes Dev. 5:2086-2095.
27. Niwa, M., S. D. Rose, and S. M. Berget. 1990. In vitro polyadenylation is stimulated by the presence of an upstream intron. Genes Dev. 4:1552-1559.
28. Nomura, N., N. Miyajima, T. Sazuka, A. Tanaka, Y. Kawarabayasi, S. Sato, T. Nagase, N. Seki, K. Ishikawa, and S. Tabata. 1994. Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1:27-35.
29. Novick, P., and R. Schekman. 1979. Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 76:1858-1862.
30. Novick, P., C. Field, and R. Schekman. 1980. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21:205-215.
31. Penn, M. D., G. Thireos, and H. Greer. 1984. Temporal analysis of general control of amino acid biosynthesis in Saccharomyces cerevisiae: role of positive regulatory genes in initiation and maintenance of mRNA derepression. Mol. Cell. Biol. 4:520-528.
32. Rose, M. D., P. Novick, J. H. Thomas, D. Botstein, and G. R. Fink. 1987. A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene 60:237-243.
33. Rymond, B. C., and M. Rosbash. 1992. Yeast pre-mRNA splicing, p. 143-192. In E. W. Jones, J. R. Pringle, and J. R. Broach (ed.), The molecular and cellular biology of the yeast Saccharomyces: gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
34. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
35. Schmitt, M. E., T. A. Brown, and B. L. Trumpower. 1990. A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res. 18:3091-3092.
36. Takao, M., M. Abramic, M. Moos, Jr., V. R. Otrin, J. C. Wooton, M. McLenigan, A. S. Levine, and M. Protic. 1993. A 127 kD component of a UV-damaged DNA-binding complex, which is defective in some xeroderma pigmentosum group E patients, is homologous to a slime mold protein. Nucleic Acids Res. 21:4111-4118.
37. Teigelkamp, S., M. McGarvey, M. Plumpton, and J. D. Beggs. 1994. The splicing factor PRP2, a putative RNA helicase. interacts directly with pre-mRNA. EMBO J. 13:888-897.
38. Thompson, C. Unpublished data.
39. Vijayraghavan, U., M. Company, and J. Abelson. 1989. Isolation and characterization of pre-mRNA splicing mutants of Saccharomyces cerevisiae. Genes Dev. 3:1206-1216.
40. Wassarman, K. M., and J. A. Steitz. 1993. Association with terminal exons in pre-mRNAs: a new role for the U1 snRNP? Genes Dev. 7:647-659.
41. Wiest, D. K., C. L. O'Day, and J. Abelson. 1996. In vitro studies of the Prp9.Prp11.Prp21 complex indicate a pathway for U2 small nuclear ribonucleoprotein activation. J. Biol. Chem. 271:33268-33276.
42. Wuestehube, L. J., R. Duden, A. Eun, S. Hamamoto, P. Korn, R. Ram, and R. Schekman. 1996. New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex. Genetics 142:393-406.