TAP (NXF1) Belongs to a Multigene Family of Putative RNA Export Factors with a Conserved Modular Architecture

REFERENCES

• Adams, M. D., Celniker, S. E., Holt, R. A., Evans, C. A., Gocayne, J. D., Amanatides, P. G., Scherer, S. E., Li, P. W., Hoskins, R. A. et al. 2000. The genome sequence of Drosophila melanogaster. Science 287:2185–2195
   PubMed Web of Science ®Google Scholar
• Almeida, F., Saffrich, R., Ansorge, W., and Carmo-Fonseca, M.. 1998. Microinjection of anti-coilin antibodies affects the structure of coiled bodies. J. Cell Biol. 142:899–912
   PubMedGoogle Scholar
• Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J.. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389–3402
   PubMed Web of Science ®Google Scholar
• Bachi, A., Braun, I. C., Rodrigues, J. P., Panté, N., Ribbeck, K., von Kobbe, C., Kutay, U., Wilm, M., Görlich, D., Carmo-Fonseca, M., and Izaurralde, E.. 2000. The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates. RNA 6:136–158
   PubMed Web of Science ®Google Scholar
• Bear, J., Tan, W., Zolotukhin, A. S., Tabernero, C., Hudson, E. A., and Felber, B. K.. 1999. Identification of novel import and export signals of human TAP, the protein that binds to the CTE element of the type D retrovirus mRNAs. Mol. Cell. Biol. 19:6306–6317
   PubMedGoogle Scholar
• Bharathi, A., Ghosh, A., Whalen, W. A., Yoon, J. H., Pu, R., Dasso, M., and Dhar, R.. 1997. The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe rae1 gene involved in nuclear export of Poly(A)+ RNA. Gene 198:251–258
   PubMedGoogle Scholar
• Black, B. E., Lévesque, L., Holaska, J. M., Wood, T. C., and Paschal, B.. 1999. Identification of an NTF2-related factor that binds RanGTP and regulates nuclear protein export. Mol. Cell. Biol. 19:8616–8624
   PubMedGoogle Scholar
• Braun, I. C., Rohrbach, E., Schmitt, C., and Izaurralde, E.. 1999. TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus. EMBO J. 18:1953–1965
   PubMedGoogle Scholar
• Brown, J. A., Bharathi, A., Ghosh, A., Whalen, W., Fitzgerald, E., and Dhar, R.. 1995. A mutation in the Schizosaccharomyces pombe rae1 gene causes defects in poly(A)+ RNA export and in the cytoskeleton. J. Biol. Chem. 270:7411–7419
   PubMed Web of Science ®Google Scholar
• The C. elegans Sequencing Consortium. Genome sequence of the nematode C. elegans: a platform for investigating biology. Science 282:2012–2018
   PubMedGoogle Scholar
• Galtier, N., Gouy, M., and Gautier, C.. 1996. 1998. SEAVIEW and PHYLO_WIN: two graphic tools for sequence alignment and molecular phylogeny. Comput. Appl. Biosci. 12:543–548
   PubMedGoogle Scholar
• Grüter, P., Tabernero, C., von Kobbe, C., Schmitt, C., Saavedra, C., Bachi, A., Wilm, M., Felber, B. K., and Izaurralde, E.. 1998. TAP, the human homologue of Mex67p, mediates CTE-dependent RNA export from the nucleus. Mol. Cell 1:649–659
   PubMed Web of Science ®Google Scholar
• Hope, T. J., Huang, X., McDonald, D., and Parslow, T. G.. 1990. Steroid-receptor fusion of the human immunodeficiency virus type 1 Rev transactivator: mapping cryptic functions of the arginine-rich motif. Proc. Natl. Acad. Sci. USA 87:7787–7791
   PubMedGoogle Scholar
• Huang, X., Hope, T. J., Bond, B. L., McDonald, D., Grahl, K., and Parslow, T. G.. 1991. Minimal Rev-response element for type 1 human immunodeficiency virus. J. Virol. 65:2131–2134
   PubMed Web of Science ®Google Scholar
• Kang, Y., and Cullen, B. R.. 1999. The human TAP protein is a nuclear mRNA export factor that contains novel RNA-binding and nucleocytoplasmic transport sequences. Genes Dev. 13:1126–1139
   PubMed Web of Science ®Google Scholar
• Kang, Y., Bogerd, H. P., and Cullen, B. R.. 2000. Analysis of cellular factors that mediate nuclear export of RNAs bearing the Mason-Pfizer monkey virus constitutive transport element. J. Virol. 74:5863–5871
   PubMedGoogle Scholar
• Katahira, J., Sträßer, K., Podtelejnikov, A., Mann, M., Jung, J. U., and Hurt, E.. 1999. The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human. EMBO J. 18:2593–2609
   PubMed Web of Science ®Google Scholar
• Kataoka, N., Yong, J., Kim, V. N., Velazquez, F., Perkinson, R. A., Wang, F., and Dreyfuss, G.. 2000. Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm. Mol. Cell 6:673–682
   PubMedGoogle Scholar
• Klebe, C., Bischoff, F. R., Ponstingl, H., and Wittinghofer, A.. 1995. Interaction of the nuclear GTP-binding protein Ran with its regulatory proteins RCC1 and RanGAP1. Biochemistry 34:639–647
   PubMedGoogle Scholar
• Kraemer, D., and Blobel, G.. 1997. mRNA binding protein mrnp 41 localizes to both nucleus and cytoplasm. Proc. Natl. Acad. Sci. USA 94:9119–9124
   PubMedGoogle Scholar
• Kutay, U., Izaurralde, E., Bischoff, F. R., Mattaj, I. W., and Görlich, D.. 1997. Dominant-negative mutants of importin-β block multiple pathways of import and export through the nuclear pore complex. EMBO J. 16:1153–1163
   PubMedGoogle Scholar
• Mattaj, I. W., and Englmeier, L.. 1998. Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem. 67:256–306
   Google Scholar
• Le Hir, H., Maquat, E. L., and Moore, J. M.. 2000. Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions. Genes Dev. 14:1098–1108
   PubMedGoogle Scholar
• Liker, E., Fernadez E., Izaurralde E., and Conti E.. The structure of the mRNA nuclear export factor TAP reveals a cis arrangement of a non-canonical RNP domain and a leucine-rich-repeat domain. EMBO J., in press.
   Google Scholar
• McGarvey, T., Rosonina, E., McCracken, S., Li, Q., Arnaout, R., Mientjes, E., Nickerson, A. J., Awrey, D., Greenblatt, J., Grosveld, G., and Blencowe, B. J.. 2000. The acute myeloid leukemia-associated protein DEK forms a splicing-dependent interaction with exon-product complexes. J. Cell Biol. 150:309–320
   PubMed Web of Science ®Google Scholar
• Morency, C. A., Neumann, J. R., and Russian, K. O.. 1987. A novel rapid assay for Chloramphenicol-acetyl transferase gene expression. BioTechniques 5:444–448
   Google Scholar
• Murphy, R., Watkins, J. L., and Wente, S. R.. 1996. GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function. Mol. Biol. Cell 7:1921–1937
   PubMedGoogle Scholar
• Nakielny, S., and Dreyfuss, G.. 1999. Transport of proteins and RNAs in and out of the nucleus. Cell 99:677–690
   PubMed Web of Science ®Google Scholar
• Parks, T. D., Leuther, K. K., Howard, E. D., Johnston, S. A., and Dougherty, W. G.. 1994. Release of proteins and peptides from fusion proteins with a recombinant plant virus proteinase. Anal. Biochem. 216:413–417
   PubMed Web of Science ®Google Scholar
• Pasquinelli, A. E., Ernst, R. K., Lund, E., Grimm, C., Zapp, M. L., Rekosh, D., Hammarskjold, M.-L., and Dahlberg, J. E.. 1997. The constitutive transport element (CTE) of Mason-Pfizer Monkey Virus (MPMV) accesses an RNA export pathway utilized by cellular messenger RNAs. EMBO J. 16:7500–7510
   PubMed Web of Science ®Google Scholar
• Pritchard, C. E. J., Fornerod, M., Kasper, L. H., and van Deursen, J. M. A.. 1999. RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains. J. Cell Biol. 145:237–253
   PubMed Web of Science ®Google Scholar
• Ryan, K., 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. A., Felber, B. K., and Izaurralde, E.. 1997. The simian retrovirus-1 constitutive transport element CTE, unlike HIV-1 RRE, utilises factors required for cellular RNA export. Curr. Biol. 7:619–628
   PubMed Web of Science ®Google Scholar
• Saitou, N., and Nei, M.. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406–425
   PubMed Web of Science ®Google Scholar
• Santos-Rosa, H., Moreno, H., Simos, G., Segref, A., Fahrenkrog, B., Panté, N., and Hurt, E.. 1998. Nuclear mRNA export requires complex formation between Mex67p and Mtr2p at the nuclear pores. Mol. Cell Biol. 18:6826–6838
   PubMed Web of Science ®Google Scholar
• Segref, A., Sharma, K., Doye, V., Hellwig, A., Huber, J., Lührmann, R., and Hurt, E.. 1997. Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores. EMBO J. 16:3256–3271
   PubMed Web of Science ®Google Scholar
• Sträßer, K., and Hurt, E.. 2000. Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export. EMBO J. 19:410–420
   PubMed Web of Science ®Google Scholar
• Sträßer, K., Baßler, J., and Hurt, E.. 2000. Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export. J. Cell Biol 150:695–706
   PubMed Web of Science ®Google Scholar
• Stutz, F., Bachi, A., Doerks, T., Braun, I. C., Séraphin, B., Wilm, M., Bork, P., and Izaurralde, E.. 2000. REF, an evolutionarily conserved family of hnRNP-like proteins, interacts with TAP/Mex67p and participates in mRNA nuclear export. RNA 6:638–650
   PubMed Web of Science ®Google Scholar
• Suyama, M., Doerks, T., Braun, I. C., Sattler, M., Izaurralde, I., and Bork, P.. 2000. Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins. EMBO Rep. 1:53–58
   PubMed Web of Science ®Google Scholar
• Tan, W., Zolotukhin A. S., Bear J., Patenaude D. J., and Felber B. K.. The mRNA export in C. elegans is mediated by Ce-TAP1, an orthologue of human TAP and S. cerevisiae Mex67p. RNA, in press.
   Google Scholar
• Thompson, J. D., Higgins, D. G., and Gibson, T. J.. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673–4680
   PubMed Web of Science ®Google Scholar
• Wu, X., Kasper L. H., Ralitsa T., Mantcheva R. T., Fontoura B. M. A., Mantchev G. T., Blobel G., and van Deursen J. M. A.. NUP98 is required for gastrulation, proper nuclear pore complex assembly and efficient protein import. J. Cell Biol., in press.
   Google Scholar