The Nuclear Pore Complex and the DEAD Box Protein Rat8p/Dbp5p Have Nonessential Features Which Appear To Facilitate mRNA Export following Heat Shock

REFERENCES

• Bailer, S. M., Balduf C., Katahira J., Podtelejnikov A., Rollenhagen C., Mann M., Pante N., and Hurt E.. 2000. Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. J. Biol. Chem. 275:23540–23548.
   PubMedGoogle Scholar
• Belgareh, N., Snay-Hodge C., Pasteau F., Dagher S., Cole C. N., and Doye V.. 1998. Functional characterization of a Nup159p-containing nuclear pore subcomplex. Mol. Biol. Cell 9:3475–3492.
   PubMedGoogle Scholar
• Craig, E. A., Gambill B. D., and Nelson R. J.. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402–414.
   PubMedGoogle Scholar
• Cullen, B. R. 2003. Nuclear RNA export. J. Cell Sci. 116:587–597.
   PubMed Web of Science ®Google Scholar
• Damelin, M., and Silver P. A.. 2000. Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex. Mol. Cell 5:133–140.
   PubMed Web of Science ®Google Scholar
• Del Priore, V., Heath C., Snay C., MacMillan A., Gorsch L., Dagher S., and Cole C.. 1997. A structure/function analysis of Rat7p/Nup159p, an essential nucleoporin of Saccharomyces cerevisiae. J. Cell Sci. 110:2987–2999.
   PubMedGoogle Scholar
• Del Priore, V., Snay C. A., Bahr A., and Cole C. N.. 1996. The product of the Saccharomyces cerevisiae RSS1 gene, identified as a high-copy suppressor of the rat7-1 temperature-sensitive allele of the RAT7/NUP159 nucleoporin, is required for efficient mRNA export. Mol. Biol. Cell 7:1601–1621.
   PubMedGoogle Scholar
• Dreyfuss, G., Kim V. N., and Kataoka N.. 2002. Messenger-RNA-binding proteins and the messages they carry. Nat. Rev. Mol. Cell Biol. 3:195–205.
   PubMed Web of Science ®Google Scholar
• Gorsch, L. C., Dockendorff T. C., and Cole C. N.. 1995. A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes. J. Cell Biol. 129:939–955.
   PubMedGoogle Scholar
• Hammell, C. M., Gross S., Zenklusen D., Heath C. V., Stutz F., Moore C., and Cole C. N.. 2002. Coupling of termination, 3′ processing, and mRNA export. Mol. Cell. Biol. 22:6441–6457.
   PubMed Web of Science ®Google Scholar
• Hodge, C. A., Colot H. V., Stafford P., and Cole C. N.. 1999. Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells. EMBO J. 18:5778–5788.
   PubMedGoogle Scholar
• Hurwitz, M. E., and Blobel G.. 1995. NUP82 is an essential yeast nucleoporin required for poly(A)+ RNA export. J. Cell Biol. 130:1275–1281.
   PubMedGoogle Scholar
• Hurwitz, M. E., Strambio-de-Castillia C., and Blobel G.. 1998. Two yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex. Proc. Natl. Acad. Sci. USA 95:11241–11245.
   PubMedGoogle Scholar
• Jankowsky, E., Gross C. H., Shuman S., and Pyle A. M.. 2000. The DExH protein NPH-II is a processive and directional motor for unwinding RNA. Nature 403:447–451.
   PubMedGoogle Scholar
• Jensen, T. H., Dower K., Libri D., and Rosbash M.. 2003. Early formation of mRNP: license for export or quality control? Mol. Cell 11:1129–1138.
   PubMed Web of Science ®Google Scholar
• Jensen, T. H., Patricio K., McCarthy T., and Rosbash M.. 2001. A block to mRNA nuclear export in S. cerevisiae leads to hyperadenylation of transcripts that accumulate at the site of transcription. Mol. Cell 7:887–898.
   PubMed Web of Science ®Google Scholar
• Jensen, T. H., and Rosbash M.. 2003. Co-transcriptional monitoring of mRNP formation. Nat. Struct. Biol. 10:10–12.
   PubMedGoogle Scholar
• Krebber, H., Taura T., Lee M. S., and Silver P. A.. 1999. Uncoupling of the hnRNP Npl3p from mRNAs during the stress-induced block in mRNA export. Genes Dev. 13:1994–2004.
   PubMedGoogle Scholar
• Lei, E. P., Krebber H., and Silver P. A.. 2001. Messenger RNAs are recruited for nuclear export during transcription. Genes Dev. 15:1771–1782.
   PubMed Web of Science ®Google Scholar
• Lei, E. P., and Silver P. A.. 2002. Protein and RNA export from the nucleus. Dev. Cell 2:261–272.
   PubMed Web of Science ®Google Scholar
• Moerschell, R. P., Tsunasawa S., and Sherman F.. 1988. Transformation of yeast with synthetic oligonucleotides. Proc. Natl. Acad. Sci. USA 85:524–528.
   PubMed Web of Science ®Google Scholar
• Petracek, M. E., and Longtine M. S.. 2002. PCR-based engineering of yeast genome. Methods Enzymol. 350:445–469.
   PubMedGoogle Scholar
• Piper, P. 1996. Induction of heat shock proteins and thermotolerance. Methods Mol. Biol. 53:313–317.
   PubMedGoogle Scholar
• Piper, P. W. 1995. The heat shock and ethanol stress responses of yeast exhibit extensive similarity and functional overlap. FEMS Microbiol. Lett. 134:121–127.
   PubMed Web of Science ®Google Scholar
• Reed, R., and Hurt E.. 2002. A conserved mRNA export machinery coupled to pre-mRNA splicing. Cell 108:523–531.
   PubMed Web of Science ®Google Scholar
• Rothstein, R. 1991. Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194:281–301.
   PubMedGoogle Scholar
• Rout, M. P., and Aitchison J. D.. 2001. The nuclear pore complex as a transport machine. J. Biol. Chem. 276:16593–16596.
   PubMed Web of Science ®Google Scholar
• Rout, M. P., Aitchison J. D., Suprapto A., Hjertaas K., Zhao Y., and Chait B. T.. 2000. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148:635–651.
   PubMed Web of Science ®Google Scholar
• Rout, M. P., and Wente S. R.. 1994. Pores for thought: nuclear pore complex proteins. Trends Cell Biol. 4:357–365.
   PubMedGoogle Scholar
• Ryan, K. J., and Wente S. R.. 2000. The nuclear pore complex: a protein machine bridging the nucleus and cytoplasm. Curr. Opin. Cell Biol. 12:361–371.
   PubMed Web of Science ®Google Scholar
• Saavedra, C., Tung K. S., Amberg D. C., Hopper A. K., and Cole C. N.. 1996. Regulation of mRNA export in response to stress in Saccharomyces cerevisiae. Genes Dev. 10:1608–1620.
   PubMed Web of Science ®Google Scholar
• Saavedra, C. A., Hammell C. M., Heath C. V., and Cole C. N.. 1997. Yeast heat shock mRNAs are exported through a distinct pathway defined by Rip1p. Genes Dev. 11:2845–2856.
   PubMedGoogle Scholar
• Schmitt, C., von Kobbe C., Bachi A., Pante N., Rodrigues J. P., Boscheron C., Rigaut G., Wilm M., Seraphin B., Carmo-Fonseca M., and Izaurralde E.. 1999. Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p. EMBO J. 18:4332–4347.
   PubMedGoogle Scholar
• Siniossoglou, S., Lutzmann M., Santos-Rosa H., Leonard K., Mueller S., Aebi U., and Hurt E.. 2000. Structure and assembly of the Nup84p complex. J. Cell Biol. 149:41–54.
   PubMed Web of Science ®Google Scholar
• Snay-Hodge, C. A., Colot H. V., Goldstein A. L., and Cole C. N.. 1998. Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export. EMBO J. 17:2663–2676.
   PubMedGoogle Scholar
• Stoffler, D., Fahrenkrog B., and Aebi U.. 1999. The nuclear pore complex: from molecular architecture to functional dynamics. Curr. Opin. Cell Biol. 11:391–401.
   PubMed Web of Science ®Google Scholar
• Strahm, Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbash M., and Stutz F.. 1999. The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p. EMBO J. 18:5761–5777.
   PubMed Web of Science ®Google Scholar
• Strawn, L. A., Shen T., Shulga N., Goldfarb D. S., and Wente S. R.. 2004. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat. Cell Biol. 6:197–206.
   PubMed Web of Science ®Google Scholar
• Stutz, F., Neville M., and Rosbash M.. 1995. Identification of a novel nuclear pore-associated protein as a functional target of the HIV-1 Rev protein in yeast. Cell 82:495–506.
   PubMedGoogle Scholar
• Suntharalingam, M., and Wente S. R.. 2003. Peering through the pore: nuclear pore complex structure, assembly, and function. Dev. Cell 4:775–789.
   PubMed Web of Science ®Google Scholar
• Tanner, N. K., and Linder P.. 2001. DExD/H box RNA helicases: from generic motors to specific dissociation functions. Mol. Cell 8:251–262.
   PubMed Web of Science ®Google Scholar
• Tseng, S. S., Weaver P. L., Liu Y., Hitomi M., Tartakoff A. M., and Chang T. H.. 1998. Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export. EMBO J. 17:2651–2662.
   PubMed Web of Science ®Google Scholar
• Wagner, J. D., Jankowsky E., Company M., Pyle A. M., and Abelson J. N.. 1998. The DEAH-box protein PRP22 is an ATPase that mediates ATP-dependent mRNA release from the spliceosome and unwinds RNA duplexes. EMBO J. 17:2926–2937.
   PubMed Web of Science ®Google Scholar
• Weis, K. 2002. Nucleocytoplasmic transport: cargo trafficking across the border. Curr. Opin. Cell Biol. 14:328–335.
   PubMed Web of Science ®Google Scholar
• Winston, F., Dolland C., and Ricupero-Hovasse S. L.. 1995. Constructing a set of convenient Saccharomyces cerevisiae strains that are isogenic to S288C. Yeast 11:53–55.
   PubMed Web of Science ®Google Scholar