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Jensen T.H., Dower K., Libri D., Rosbash M. Early formation of mRNP: license for export or quality control? Mol Cell. 11:2003;1129-1138
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Bentley D. The mRNA assembly line: transcription and processing machines in the same factory. Curr Opin Cell Biol. 14:2002;336-342
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Kwek K.Y., Murphy S., Furger A., Thomas B., O'Gorman W., Kimura H., Proudfoot N.J., Akoulitchev A. U1 snRNA associates with TFIIH and regulates transcriptional initiation. Nat Struct Biol. 9:2002;800-805
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Manley J.L. Nuclear coupling: RNA processing reaches back to transcription. Nat Struct Biol. 9:2002;790-791
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Jensen T.H., Rosbash M. Co-transcriptional monitoring of mRNP formation. Nat Struct Biol. 10:2003;10-12
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The interplay of nuclear mRNP assembly, mRNA surveillance and export
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Stutz F., Izaurralde E. The interplay of nuclear mRNP assembly, mRNA surveillance and export. Trends Cell Biol. 13:2003;319-327
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Stutz, F.1
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A conserved mRNA export machinery coupled to pre-mRNA splicing
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Reed R., Hurt E. A conserved mRNA export machinery coupled to pre-mRNA splicing. Cell. 108:2002;523-531
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Reed, R.1
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0037175374
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REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export
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Using RNA interference in Drosophila cells, the authors show that REF1, as well as other components of the EJC, are not essential for mRNA export, indicating that mRNA export factors can be recruited independently of splicing.
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Gatfield D., Izaurralde E. REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export. J Cell Biol. 159:2002;579-588 Using RNA interference in Drosophila cells, the authors show that REF1, as well as other components of the EJC, are not essential for mRNA export, indicating that mRNA export factors can be recruited independently of splicing.
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Gatfield, D.1
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Gatfield D., Le Hir H., Schmitt C., Braun I.C., Kocher T., Wilm M., Izaurralde E. The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export in Drosophila. Curr Biol. 11:2001;1716-1721
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Gatfield, D.1
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Wilm, M.6
Izaurralde, E.7
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13
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0037566678
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Genome-wide analysis of nuclear mRNA export pathways in Drosophila
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This is the first global study of mRNA export pathways in higher eukaryotes. Using RNAi and DNA micro-arrays, the authors show that the export factors NXF1, NXT1 and UAP56 in Drosophila act in the same pathway and are essential for the export of most transcripts.
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Herold A., Teixeira L., Izaurralde E. Genome-wide analysis of nuclear mRNA export pathways in Drosophila. EMBO J. 22:2003;2472-2483 This is the first global study of mRNA export pathways in higher eukaryotes. Using RNAi and DNA micro-arrays, the authors show that the export factors NXF1, NXT1 and UAP56 in Drosophila act in the same pathway and are essential for the export of most transcripts.
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EMBO J
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Herold, A.1
Teixeira, L.2
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0038381687
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The Ref/Aly proteins are dispensable for mRNA export and development in Caenorhabditis elegans
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Using RNAi, the authors show that REF proteins are dispensable for mRNA export in C. elegans, suggesting the existence of additional mRNA export adaptors in this organism.
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Longman D., Johnstone I.L., Caceres J.F. The Ref/Aly proteins are dispensable for mRNA export and development in Caenorhabditis elegans. RNA. 9:2003;881-891 Using RNAi, the authors show that REF proteins are dispensable for mRNA export in C. elegans, suggesting the existence of additional mRNA export adaptors in this organism.
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RNA
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Longman, D.1
Johnstone, I.L.2
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SR splicing factors serve as adapter proteins for TAP-dependent mRNA export
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Huang Y., Gattoni R., Stevenin J., Steitz J.A. SR splicing factors serve as adapter proteins for TAP-dependent mRNA export. Mol Cell. 11:2003;837-843
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Mol Cell
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Huang, Y.1
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16
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0037313537
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Genome-wide analysis of RNA-protein interactions illustrates specificity of the mRNA export machinery
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This genome-wide analysis shows that only a small fraction of yeast transcripts binds Yra1p, Mex67p or both, suggesting the existence of additional mRNA export factors. Evidence suggests that some export factors preferentially associate with co-regulated transcripts, perhaps through interaction with the transcriptional machinery.
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Hieronymus H., Silver P.A. Genome-wide analysis of RNA-protein interactions illustrates specificity of the mRNA export machinery. Nat Genet. 33:2003;155-161 This genome-wide analysis shows that only a small fraction of yeast transcripts binds Yra1p, Mex67p or both, suggesting the existence of additional mRNA export factors. Evidence suggests that some export factors preferentially associate with co-regulated transcripts, perhaps through interaction with the transcriptional machinery.
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Nat Genet
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Hieronymus, H.1
Silver, P.A.2
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0842288796
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The Glc7p nuclear phosphatase promotes mRNA export by facilitating association of Mex67p with mRNA
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This study shows that the yeast shuttling SR-like protein Npl3p directly interacts with Mex67p and that this association requires Npl3p dephosphorylation. The data provide evidence that dephosphorylation of Npl3p and perhaps other factors by the phosphatase Glc7p, participates in mRNA export regulation by controlling the recruitment of Mex67p to mRNP complexes.
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Gilbert W., Guthrie C. The Glc7p nuclear phosphatase promotes mRNA export by facilitating association of Mex67p with mRNA. Mol Cell. 13:2004;201-212 This study shows that the yeast shuttling SR-like protein Npl3p directly interacts with Mex67p and that this association requires Npl3p dephosphorylation. The data provide evidence that dephosphorylation of Npl3p and perhaps other factors by the phosphatase Glc7p, participates in mRNA export regulation by controlling the recruitment of Mex67p to mRNP complexes.
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Mol Cell
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Gilbert, W.1
Guthrie, C.2
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The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
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Le Hir H., Gatfield D., Izaurralde E., Moore M.J. The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. EMBO J. 19:2001;6860-6869
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Le Hir, H.1
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Coupling transcription, splicing and mRNA export
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Reed R. Coupling transcription, splicing and mRNA export. Curr Opin Cell Biol. 15:2003;326-331
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Curr Opin Cell Biol
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Linder P., Stutz F. mRNA export: travelling with DEAD box proteins. Curr Biol. 11:2001;R961-963
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Linder, P.1
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21
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0141706348
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Exon junction complexes mediate the enhancing effect of splicing on mRNA expression
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This study uses artificial tethering of EJC components to non-intron containing transcripts to show that the EJC, deposited normally on mRNA as a result of splicing, enhances 3′-end processing/polyadenylation and translation. The data show that the EJC is primarily responsible for the positive effect of splicing on gene expression in mammalian cells, by stimulating translation rather than mRNA export.
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Wiegand H.L., Lu S., Cullen B.R. Exon junction complexes mediate the enhancing effect of splicing on mRNA expression. Proc Natl Acad Sci USA. 100:2003;11327-11332 This study uses artificial tethering of EJC components to non-intron containing transcripts to show that the EJC, deposited normally on mRNA as a result of splicing, enhances 3′-end processing/polyadenylation and translation. The data show that the EJC is primarily responsible for the positive effect of splicing on gene expression in mammalian cells, by stimulating translation rather than mRNA export.
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Proc Natl Acad Sci USA
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Wiegand, H.L.1
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22
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0942268832
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Splicing enhances translation in mammalian cells: An additional function of the exon junction complex
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Using artificial tethering of EJC components to reporter transcripts, this study shows that the EJC, deposited on mRNA as a result of splicing, promotes mRNA polysome association and stimulates translation.
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Nott A., Le Hir H., Moore M.J. Splicing enhances translation in mammalian cells: an additional function of the exon junction complex. Genes Dev. 18:2004;210-222 Using artificial tethering of EJC components to reporter transcripts, this study shows that the EJC, deposited on mRNA as a result of splicing, promotes mRNA polysome association and stimulates translation.
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Genes Dev
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Nott, A.1
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Messenger RNAs are recruited for nuclear export during transcription
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Lei E.P., Krebber H., Silver P.A. Messenger RNAs are recruited for nuclear export during transcription. Genes Dev. 15:2001;1771-1782
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Genes Dev
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Lei, E.P.1
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0034329461
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A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae
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Chavez S., Beilharz T., Rondon A.G., Erdjument-Bromage H., Tempst P., Svejstrup J.Q., Lithgow T., Aguilera A. A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae. Embo J. 19:2000;5824-5834
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Chavez, S.1
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Tempst, P.5
Svejstrup, J.Q.6
Lithgow, T.7
Aguilera, A.8
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25
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0036889142
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Interactions between mRNA export commitment, 3′-end quality control, and nuclear degradation
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This paper describes genetic interactions between TREX and the nuclear exosome. Mutations in TREX result in low levels of 3′-end-truncated HSP104 transcripts retained in nuclear foci. The data show that the exosome component Rrp6p is implicated in the sequestration and degradation of incorrectly assembled mRNP complexes.
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Libri D., Dower K., Boulay J., Thomsen R., Rosbash M., Jensen T.H. Interactions between mRNA export commitment, 3′-end quality control, and nuclear degradation. Mol Cell Biol. 22:2002;8254-8266 This paper describes genetic interactions between TREX and the nuclear exosome. Mutations in TREX result in low levels of 3′-end-truncated HSP104 transcripts retained in nuclear foci. The data show that the exosome component Rrp6p is implicated in the sequestration and degradation of incorrectly assembled mRNP complexes.
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Mol Cell Biol
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Libri, D.1
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Boulay, J.3
Thomsen, R.4
Rosbash, M.5
Jensen, T.H.6
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26
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0037118052
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TREX is a conserved complex coupling transcription with messenger RNA export
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This study identifies TREX, a new complex in yeast and mammals. TREX contains proteins implicated in transcription elongation (THO complex) mRNA export factors (Yra1p, Sub2p) and Tex1p, a protein of unknown function. TREX may facilitate the co-transcriptional loading of mRNA export factors.
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Strasser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M., Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R., et al. TREX is a conserved complex coupling transcription with messenger RNA export. Nature. 417:2002;304-308 This study identifies TREX, a new complex in yeast and mammals. TREX contains proteins implicated in transcription elongation (THO complex) mRNA export factors (Yra1p, Sub2p) and Tex1p, a protein of unknown function. TREX may facilitate the co-transcriptional loading of mRNA export factors.
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Nature
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Strasser, K.1
Masuda, S.2
Mason, P.3
Pfannstiel, J.4
Oppizzi, M.5
Rodriguez-Navarro, S.6
Rondon, A.G.7
Aguilera, A.8
Struhl, K.9
Reed, R.10
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27
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0036889334
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Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p
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This study identifies genetic interactions between Yra1p and Sub2p, THO and the nuclear exosome. It shows that the THO component Hpr1p directly interacts with Sub2p and facilitates its co-transcriptional recruitment. In addition, transcripts assembled in a yra1 mutant accumulate in nuclear foci and are degraded by the exosome.
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Zenklusen D., Vinciguerra P., Wyss J.C., Stutz F. Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p. Mol Cell Biol. 22:2002;8241-8253 This study identifies genetic interactions between Yra1p and Sub2p, THO and the nuclear exosome. It shows that the THO component Hpr1p directly interacts with Sub2p and facilitates its co-transcriptional recruitment. In addition, transcripts assembled in a yra1 mutant accumulate in nuclear foci and are degraded by the exosome.
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Mol Cell Biol
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Zenklusen, D.1
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Wyss, J.C.3
Stutz, F.4
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28
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18744370194
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The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores
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The authors describe a novel complex Thp1p-Sac3p, implicated in mRNA export, and show that Sac3p interacts with Mex67p and nucleoporins. Thp1p-Sac3p may be recruited to mRNPs at an early stage and subsequently function in docking mRNP complexes to the nuclear face of the NPC via interaction with Mex67p and FG-nucleoporins.
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Fischer T., Strasser K., Racz A., Rodriguez-Navarro S., Oppizzi M., Ihrig P., Lechner J., Hurt E. The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores. Embo J. 21:2002;5843-5852 The authors describe a novel complex Thp1p-Sac3p, implicated in mRNA export, and show that Sac3p interacts with Mex67p and nucleoporins. Thp1p-Sac3p may be recruited to mRNPs at an early stage and subsequently function in docking mRNP complexes to the nuclear face of the NPC via interaction with Mex67p and FG-nucleoporins.
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Embo J
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Fischer, T.1
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Rodriguez-Navarro, S.4
Oppizzi, M.5
Ihrig, P.6
Lechner, J.7
Hurt, E.8
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29
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0035156427
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A new hyperrecombination mutation identifies a novel yeast gene, THP1, connecting transcription elongation with mitotic recombination
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Gallardo M., Aguilera A. A new hyperrecombination mutation identifies a novel yeast gene, THP1, connecting transcription elongation with mitotic recombination. Genetics. 157:2001;79-89
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Gallardo, M.1
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0037342695
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Sac3 is an mRNA export factor that localizes to cytoplasmic fibrils of nuclear pore complex
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Lei E.P., Stern C.A., Fahrenkrog B., Krebber H., Moy T.I., Aebi U., Silver P.A. Sac3 is an mRNA export factor that localizes to cytoplasmic fibrils of nuclear pore complex. Mol Biol Cell. 14:2003;836-847
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Lei, E.P.1
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Moy, T.I.5
Aebi, U.6
Silver, P.A.7
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31
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10744233477
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Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery
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This study identified Sus1p, which interacts with SAGA, a complex implicated in transcription initiation, and suggests that Sus1p connects SAGA to Thp1-Sac3p, an NPC-associated complex involved in mRNA export. Sac3p may be regulated by SAGA-dependent acetylation.
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Rodriguez-Navarro S., Fischer T., Luo M.J., Antunez O., Perez-Ortin J.E., Reed R., Hurt E. Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Cell. 116:2004;75-86 This study identified Sus1p, which interacts with SAGA, a complex implicated in transcription initiation, and suggests that Sus1p connects SAGA to Thp1-Sac3p, an NPC-associated complex involved in mRNA export. Sac3p may be regulated by SAGA-dependent acetylation.
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Cell
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Rodriguez-Navarro, S.1
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Redundant roles for the TFIID and SAGA complexes in global transcription
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Lee T.I., Causton H.C., Holstege F.C., Shen W.C., Hannett N., Jennings E.G., Winston F., Green M.R., Young R.A. Redundant roles for the TFIID and SAGA complexes in global transcription. Nature. 405:2000;701-704
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TOM1p, a yeast hect-domain protein which mediates transcriptional regulation through the ADA/SAGA coactivator complexes
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Saleh A., Collart M., Martens J.A., Genereaux J., Allard S., Cote J., Brandl C.J. TOM1p, a yeast hect-domain protein which mediates transcriptional regulation through the ADA/SAGA coactivator complexes. J Mol Biol. 282:1998;933-946
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A putative ubiquitin ligase required for efficient mRNA export differentially affects hnRNP transport
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Duncan K., Umen J.G., Guthrie C. A putative ubiquitin ligase required for efficient mRNA export differentially affects hnRNP transport. Curr Biol. 10:2000;687-696
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Duncan, K.1
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Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p
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Green D.M., Marfatia K.A., Crafton E.B., Zhang X., Cheng X., Corbett A.H. Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p. J Biol Chem. 277:2002;7752-7760
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0038605527
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Nab2p and the Thp1p-Sac3p complex functionally interact at the interface between transcription and mRNA metabolism
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Gallardo M., Luna R., Erdjument-Bromage H., Tempst P., Aguilera A. Nab2p and the Thp1p-Sac3p complex functionally interact at the interface between transcription and mRNA metabolism. J Biol Chem. 278:2003;24225-24232
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0042812051
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The HECT ubiquitin ligase Rsp5p is required for proper nuclear export of mRNA in Saccharomyces cerevisiae
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Rodriguez M.S., Gwizdek C., Haguenauer-Tsapis R., Dargemont C. The HECT ubiquitin ligase Rsp5p is required for proper nuclear export of mRNA in Saccharomyces cerevisiae. Traffic. 4:2003;566-575
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Formation and nuclear export of tRNA, rRNA and mRNA is regulated by the ubiquitin ligase Rsp5p
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Neumann S., Petfalski E., Brugger B., Grosshans H., Wieland F., Tollervey D., Hurt E. Formation and nuclear export of tRNA, rRNA and mRNA is regulated by the ubiquitin ligase Rsp5p. EMBO Rep. 4:2003;1156-1162
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Gilbert W., Siebel C.W., Guthrie C. Phosphorylation by Sky1p promotes Npl3p shuttling and mRNA dissociation. RNA. 7:2001;302-313
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Directing mRNA export
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Izaurralde E. Directing mRNA export. Nat Struct Mol Biol. 11:2004;210-212
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(2004)
Nat Struct Mol Biol
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Izaurralde, E.1
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41
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0035807308
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Quality control of mRNA 3′-end processing is linked to the nuclear exosome
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Hilleren P., McCarthy T., Rosbash M., Parker R., Jensen T.H. Quality control of mRNA 3′-end processing is linked to the nuclear exosome. Nature. 413:2001;538-542
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Nature
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Hilleren, P.1
McCarthy, T.2
Rosbash, M.3
Parker, R.4
Jensen, T.H.5
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0034544815
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Pre-mRNA processing factors are required for nuclear export
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Brodsky A.S., Silver P.A. Pre-mRNA processing factors are required for nuclear export. Rna. 6:2000;1737-1749
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Rna
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Brodsky, A.S.1
Silver, P.A.2
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43
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0036723624
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Coupling of termination, 3′ processing, and mRNA export
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Using yeast mutants, these authors show that 3' end cleavage, polyadenylation, transcription termination and export are tightly linked. The similarity of phenotypes of mRNA export mutants and 3' processing mutants indicates that some factors from each process may mechanistically interact to couple mRNA processing and export.
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Hammell C.M., Gross S., Zenklusen D., Heath C.V., Stutz F., Moore C., Cole C.N. Coupling of termination, 3′ processing, and mRNA export. Mol Cell Biol. 22:2002;6441-6457 Using yeast mutants, these authors show that 3' end cleavage, polyadenylation, transcription termination and export are tightly linked. The similarity of phenotypes of mRNA export mutants and 3' processing mutants indicates that some factors from each process may mechanistically interact to couple mRNA processing and export.
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(2002)
Mol Cell Biol
, vol.22
, pp. 6441-6457
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Hammell, C.M.1
Gross, S.2
Zenklusen, D.3
Heath, C.V.4
Stutz, F.5
Moore, C.6
Cole, C.N.7
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44
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0036252704
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T7 RNA polymerase-directed transcripts are processed in yeast and link 3′ end formation to mRNA nuclear export
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The authors study the export of a transcript generated by T7 RNA polymerase in yeast and show that transcription by RNA polymerase II is not required for nuclear exit, but that 3′ end processing is both necessary and sufficient for mRNA release and export.
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Dower K., Rosbash M. T7 RNA polymerase-directed transcripts are processed in yeast and link 3′ end formation to mRNA nuclear export. RNA. 8:2002;686-697 The authors study the export of a transcript generated by T7 RNA polymerase in yeast and show that transcription by RNA polymerase II is not required for nuclear exit, but that 3′ end processing is both necessary and sufficient for mRNA release and export.
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(2002)
RNA
, vol.8
, pp. 686-697
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Dower, K.1
Rosbash, M.2
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45
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0037007218
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Dual requirement for yeast hnRNP Nab2p in mRNA poly(A) tail length control and nuclear export
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This paper looks at the role of Nab2p in polyA tail length regulation in vivo and in vitro, and suggests that Nab2p links termination of polyadenylation to export.
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Hector R.E., Nykamp K.R., Dheur S., Anderson J.T., Non P.J., Urbinati C.R., Wilson S.M., Minvielle-Sebastia L., Swanson M.S. Dual requirement for yeast hnRNP Nab2p in mRNA poly(A) tail length control and nuclear export. EMBO J. 21:2002;1800-1810 This paper looks at the role of Nab2p in polyA tail length regulation in vivo and in vitro, and suggests that Nab2p links termination of polyadenylation to export.
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(2002)
EMBO J
, vol.21
, pp. 1800-1810
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Hector, R.E.1
Nykamp, K.R.2
Dheur, S.3
Anderson, J.T.4
Non, P.J.5
Urbinati, C.R.6
Wilson, S.M.7
Minvielle-Sebastia, L.8
Swanson, M.S.9
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46
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0037470143
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Domain analysis of the Saccharomyces cerevisiae heterogeneous nuclear ribonucleoprotein, Nab2p. Dissecting the requirements for Nab2p-facilitated poly(A) RNA export
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Marfatia K.A., Crafton E.B., Green D.M., Corbett A.H. Domain analysis of the Saccharomyces cerevisiae heterogeneous nuclear ribonucleoprotein, Nab2p. Dissecting the requirements for Nab2p-facilitated poly(A) RNA export. J Biol Chem. 278:2003;6731-6740
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J Biol Chem
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Marfatia, K.A.1
Crafton, E.B.2
Green, D.M.3
Corbett, A.H.4
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47
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0041832131
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Localization of nuclear retained mRNAs in Saccharomyces cerevisiae
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In situ hybridization is used to localize nuclear retained HSP104 transcripts with respect to different tagged genomic loci. The data show that HSP104 nuclear foci formed in mRNA export mutants are at or close to the transcription site.
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Thomsen R., Libri D., Boulay J., Rosbash M., Jensen T.H. Localization of nuclear retained mRNAs in Saccharomyces cerevisiae. RNA. 9:2003;1049-1057 In situ hybridization is used to localize nuclear retained HSP104 transcripts with respect to different tagged genomic loci. The data show that HSP104 nuclear foci formed in mRNA export mutants are at or close to the transcription site.
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(2003)
RNA
, vol.9
, pp. 1049-1057
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Thomsen, R.1
Libri, D.2
Boulay, J.3
Rosbash, M.4
Jensen, T.H.5
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48
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0037180825
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The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila
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Chromatin immunoprecipitation experiments show that the nuclear exosome is recruited to actively transcribed genes. The exosome physically interacts with RNA polymerase II and the elongation factors Spt5 and Spt6 and retains its activity when engaged in these interactions. The data suggest that the exosome monitors and degrades mRNA co-transcriptionally.
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Andrulis E.D., Werner J., Nazarian A., Erdjument-Bromage H., Tempst P., Lis J.T. The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila. Nature. 420:2002;837-841 Chromatin immunoprecipitation experiments show that the nuclear exosome is recruited to actively transcribed genes. The exosome physically interacts with RNA polymerase II and the elongation factors Spt5 and Spt6 and retains its activity when engaged in these interactions. The data suggest that the exosome monitors and degrades mRNA co-transcriptionally.
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(2002)
Nature
, vol.420
, pp. 837-841
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Andrulis, E.D.1
Werner, J.2
Nazarian, A.3
Erdjument-Bromage, H.4
Tempst, P.5
Lis, J.T.6
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49
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0034808138
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Hpr1 is preferentially required for transcription of either long or G+C-rich DNA sequences in Saccharomyces cerevisiae
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Chavez S., Garcia-Rubio M., Prado F., Aguilera A. Hpr1 is preferentially required for transcription of either long or G+C-rich DNA sequences in Saccharomyces cerevisiae. Mol Cell Biol. 21:2001;7054-7064
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(2001)
Mol Cell Biol
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Chavez, S.1
Garcia-Rubio, M.2
Prado, F.3
Aguilera, A.4
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50
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0031439267
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The yeast HPR1 gene has a functional role in transcriptional elongation that uncovers a novel source of genome instability
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Chavez S., Aguilera A. The yeast HPR1 gene has a functional role in transcriptional elongation that uncovers a novel source of genome instability. Genes Dev. 11:1997;3459-3470
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Genes Dev
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Chavez, S.1
Aguilera, A.2
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51
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0141819093
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Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination
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This paper indicates that mRNAs formed in the absence of THO tend to form DNA:RNA hybrids, creating an obstacle for the next polymerase and resulting in an elongation block. Co-transcriptional self-cleavage of the nascent mRNA by a hammerhead ribozyme and over-expression of RNAse H1 eliminate DNA:RNA hybrids as well as the elongation and hyper-recombination phenotypes. THO/TREX may prevent the formation of DNA:RNA hybrids during elongation by promoting efficient mRNP assembly.
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Huertas P., Aguilera A. Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination. Mol Cell. 12:2003;711-721 This paper indicates that mRNAs formed in the absence of THO tend to form DNA:RNA hybrids, creating an obstacle for the next polymerase and resulting in an elongation block. Co-transcriptional self-cleavage of the nascent mRNA by a hammerhead ribozyme and over-expression of RNAse H1 eliminate DNA:RNA hybrids as well as the elongation and hyper-recombination phenotypes. THO/TREX may prevent the formation of DNA:RNA hybrids during elongation by promoting efficient mRNP assembly.
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(2003)
Mol Cell
, vol.12
, pp. 711-721
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Huertas, P.1
Aguilera, A.2
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52
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0036469913
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The connection between transcription and genomic instability
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Aguilera A. The connection between transcription and genomic instability. EMBO J. 21:2002;195-201
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(2002)
EMBO J
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Aguilera, A.1
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53
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0036645687
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The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability
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mRNA export mutants including sub2, yra1, mex67 and mtr2 show similar transcription elongation defects and hyper-recombination phenotypes as THO mutants. These results indicate a tight link between elongation and early mRNP assembly mediated by THO and mRNA export proteins, which also influences genome stability.
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Jimeno S., Rondon A.G., Luna R., Aguilera A. The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability. EMBO J. 21:2002;3526-3535 mRNA export mutants including sub2, yra1, mex67 and mtr2 show similar transcription elongation defects and hyper-recombination phenotypes as THO mutants. These results indicate a tight link between elongation and early mRNP assembly mediated by THO and mRNA export proteins, which also influences genome stability.
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(2002)
EMBO J
, vol.21
, pp. 3526-3535
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Jimeno, S.1
Rondon, A.G.2
Luna, R.3
Aguilera, A.4
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54
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0037884974
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An early function during transcription for the yeast mRNA export factor Dbp5p/Rat8p suggested by its genetic and physical interactions with transcription factor IIH components
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Estruch F., Cole C.N. An early function during transcription for the yeast mRNA export factor Dbp5p/Rat8p suggested by its genetic and physical interactions with transcription factor IIH components. Mol Biol Cell. 14:2003;1664-1676
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(2003)
Mol Biol Cell
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, pp. 1664-1676
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Estruch, F.1
Cole, C.N.2
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55
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0034614558
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Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p
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Kosova B., Pante N., Rollenhagen C., Podtelejnikov A., Mann M., Aebi U., Hurt E. Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p. J Biol Chem. 275:2000;343-350
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J Biol Chem
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Kosova, B.1
Pante, N.2
Rollenhagen, C.3
Podtelejnikov, A.4
Mann, M.5
Aebi, U.6
Hurt, E.7
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56
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0033535342
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Proteins connecting the nuclear pore complex with the nuclear interior
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Strambio-de-Castillia C., Blobel G., Rout M.P. Proteins connecting the nuclear pore complex with the nuclear interior. J Cell Biol. 144:1999;839-855
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J Cell Biol
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Strambio-De-Castillia, C.1
Blobel, G.2
Rout, M.P.3
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57
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0742304306
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Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1
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In this paper, genetic, biochemical and in situ hybridization experiments show that Mlp1p contributes to mRNP surveillance by specifically retaining unspliced pre-mRNAs within the nucleus. The study shows that Mlp proteins are asymmetrically distributed around the nuclear envelope.
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Galy V., Gadal O., Fromont-Racine M., Romano A., Jacquier A., Nehrbass U. Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1. Cell. 116:2004;63-73 In this paper, genetic, biochemical and in situ hybridization experiments show that Mlp1p contributes to mRNP surveillance by specifically retaining unspliced pre-mRNAs within the nucleus. The study shows that Mlp proteins are asymmetrically distributed around the nuclear envelope.
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(2004)
Cell
, vol.116
, pp. 63-73
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Galy, V.1
Gadal, O.2
Fromont-Racine, M.3
Romano, A.4
Jacquier, A.5
Nehrbass, U.6
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58
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0037417959
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The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export
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This paper shows that Nab2p directly interacts with the C-terminal domain of Mlp1p and that over-expression of Mlp1p blocks both polyA+ and Nab2p export, suggesting it may function as a docking site for Nab2p-associated mRNA.
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Green D.M., Johnson C.P., Hagan H., Corbett A.H. The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export. Proc Natl Acad Sci USA. 100:2003;1010-1015 This paper shows that Nab2p directly interacts with the C-terminal domain of Mlp1p and that over-expression of Mlp1p blocks both polyA+ and Nab2p export, suggesting it may function as a docking site for Nab2p-associated mRNA.
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(2003)
Proc Natl Acad Sci USA
, vol.100
, pp. 1010-1015
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Green, D.M.1
Johnson, C.P.2
Hagan, H.3
Corbett, A.H.4
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59
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0037205232
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Chromatin boundaries in budding yeast: The nuclear pore connection
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This paper shows that nuclear transport receptors artificially tethered to a genomic locus have boundary activity (BA), i.e. they establish non-silenced domains. BA depends on the nucleoporin Nup2p, which anchors the transport receptor to the NPC. The data indicate that physical tethering of genomic loci to the NPC can dramatically alter gene activity.
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Ishii K., Arib G., Lin C., Van Houwe G., Laemmli U.K. Chromatin boundaries in budding yeast: the nuclear pore connection. Cell. 109:2002;551-562 This paper shows that nuclear transport receptors artificially tethered to a genomic locus have boundary activity (BA), i.e. they establish non-silenced domains. BA depends on the nucleoporin Nup2p, which anchors the transport receptor to the NPC. The data indicate that physical tethering of genomic loci to the NPC can dramatically alter gene activity.
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(2002)
Cell
, vol.109
, pp. 551-562
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Ishii, K.1
Arib, G.2
Lin, C.3
Van Houwe, G.4
Laemmli, U.K.5
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