Ed Hurt

An Endoribonuclease Functionally Linked to Perinuclear mRNP Quality Control Associates with the Nuclear Pore Complexes (2009)

Michal Skružný, Claudia Schneider, Attila Rácz, Julan Weng, David Tollervey, Ed Hurt

Nuclear mRNA export is a crucial step in eukaryotic gene expression, which is in yeast coupled to cotranscriptional messenger ribonucleoprotein particle (mRNP) assembly and surveillance. Several...

Recruitment of the human TREX complex to mRNA during splicing (2005)

Masuda, Seiji, Das, Rita, Cheng, Hong, Hurt, Ed, Dorman, Nijsje, Reed, Robin

In yeast, the TREX complex contains the THO transcription elongation complex, which functions in direct cotranscriptional recruitment of the mRNA export proteins Sub2 and Yra1 to nascent transcripts....

Cloning and characterization of the Schizosaccharomyces pombe tRNA:pseudouridine synthase Pus1p (2000)

Hellmuth, Klaus, Grosjean, Henri, Motorin, Yuri, Deinert, Karina, Hurt, Ed, Simos, George

Saccharomyces cerevisiae cells that carry deletions in both the LOS1 (a tRNA export receptor) and the PUS1 (a tRNA:pseudouridine synthase) genes exhibit a thermosensitive growth defect. A...

Nup93, a Vertebrate Homologue of Yeast Nic96p, Forms a Complex with a Novel 205-kDa Protein and Is Required for Correct Nuclear Pore Assembly

Grandi, Paola, Dang, Tam, Pané, Nelly, Shevchenko, Andrej, Mann, Matthias, Forbes, Douglass, ...

Yeast and vertebrate nuclear pores display significant morphological similarity by electron microscopy, but sequence similarity between the respective proteins has been more difficult to observe....

Yeast Ran-Binding Protein 1 (Yrb1) Shuttles between the Nucleus and Cytoplasm and Is Exported from the Nucleus via a CRM1 (XPO1)-Dependent Pathway

Künzler, Markus, Gerstberger, Thomas, Stutz, Françoise, Bischoff, F. Ralf, Hurt, Ed

The RanGTP-binding protein RanBP1, which is located in the cytoplasm, has been implicated in release of nuclear export complexes from the cytoplasmic side of the nuclear pore complex. Here we show...

The Nsp1p Carboxy-Terminal Domain Is Organized into Functionally Distinct Coiled-Coil Regions Required for Assembly of Nucleoporin Subcomplexes and Nucleocytoplasmic Transport

Bailer, Susanne M., Balduf, Carolin, Hurt, Ed

Nucleoporin Nsp1p, which has four predicted coiled-coil regions (coils 1 to 4) in the essential carboxy-terminal domain, is unique in that it is part of two distinct nuclear pore complex (NPC)...

Nuclear Export of 60S Ribosomal Subunits Depends on Xpo1p and Requires a Nuclear Export Sequence-Containing Factor, Nmd3p, That Associates with the Large Subunit Protein Rpl10p

Gadal, Olivier, Strauß, Daniela, Kessl, Jacques, Trumpower, Bernard, Tollervey, David, Hurt, Ed

Nuclear export of ribosomes requires a subset of nucleoporins and the Ran system, but specific transport factors have not been identified. Using a large subunit reporter (Rpl25p-eGFP), we have...

Yeast Los1p Has Properties of an Exportin-Like Nucleocytoplasmic Transport Factor for tRNA

Hellmuth, Klaus, Lau, Denise M., Bischoff, F. Ralf, Künzler, Markus, Hurt, Ed, Simos, George

Saccharomyces cerevisiae Los1p, which is genetically linked to the nuclear pore protein Nsp1p and several tRNA biogenesis factors, was recently grouped into the family of importin/karyopherin-β-like...

Nuclear mRNA Export Requires Complex Formation between Mex67p and Mtr2p at the Nuclear Pores

Santos-Rosa, Helena, Moreno, Horacio, Simos, George, Segref, Alexandra, Fahrenkrog, Birthe, Panté, Nelly, ...

We have identified between Mex67p and Mtr2p a complex which is essential for mRNA export. This complex, either isolated from yeast or assembled in Escherichia coli, can bind in vitro to RNA through...

Cloning and characterization of the Schizosaccharomyces pombe tRNA:pseudouridine synthase Pus1p

Hellmuth, Klaus, Grosjean, Henri, Motorin, Yuri, Deinert, Karina, Hurt, Ed, Simos, George

Saccharomyces cerevisiae cells that carry deletions in both the LOS1 (a tRNA export receptor) and the PUS1 (a tRNA:pseudouridine synthase) genes exhibit a thermosensitive growth defect. A...

A nuclear AAA-type ATPase (Rix7p) is required for biogenesis and nuclear export of 60S ribosomal subunits

Gadal, Olivier, Strauß, Daniela, Braspenning, Joris, Hoepfner, Dominic, Petfalski, Elisabeth, Philippsen, Peter, ...

Ribosomal precursor particles are assembled in the nucleolus before export into the cytoplasm. Using a visual assay for nuclear accumulation of 60S subunits, we have isolated several...

Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins

Lutzmann, Malik, Kunze, Ruth, Buerer, Andrea, Aebi, Ueli, Hurt, Ed

Now that it is likely that all yeast nucleoporins are known, one of the ultimate goals is the in vitro assembly of the entire nuclear pore complex from its ∼30 individual components. Here, we...

60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm

Nissan, Tracy A., Baßler, Jochen, Petfalski, Elisabeth, Tollervey, David, Hurt, Ed

60S ribosomes undergo initial assembly in the nucleolus before export to the cytoplasm and recent analyses have identified several nucleolar pre-60S particles. To unravel the steps in the pathway of...

The mRNA export machinery requires the novel Sac3p–Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores

Fischer, Tamás, Sträßer, Katja, Rácz, Attila, Rodriguez-Navarro, Susana, Oppizzi, Marisa, Ihrig, Petra, ...

Yra1p and Sub2p are components of the TREX complex, which couples transcription elongation with nuclear export of mRNAs. Here, we report a genetic interaction between Yra1p and a conserved protein...

The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes

Schäfer, Thorsten, Strauß, Daniela, Petfalski, Elisabeth, Tollervey, David, Hurt, Ed

Recent reports have increased our knowledge of the consecutive steps during 60S ribosome biogenesis substantially, but 40S subunit formation is less well understood. Here, we investigate the...

Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export

Sträßer, Katja, Hurt, Ed

Mex67p and Mtr2p constitute an essential mRNA export complex that interacts with poly(A)+ RNA and nuclear pore proteins. We have identified Yra1p, an intranuclear protein with in vitro RNA–RNA...

An aminoacylation-dependent nuclear tRNA export pathway in yeast

Grosshans, Helge, Hurt, Ed, Simos, George

Yeast Los1p, the homolog of human exportin-t, mediates nuclear export of tRNA. Using fluorescence in situ hybridization, we could show that the export of some intronless tRNA species is not...

Cotranscriptional recruitment of the serine-arginine-rich (SR)-like proteins Gbp2 and Hrb1 to nascent mRNA via the TREX complex

Hurt, Ed, Luo, Ming-juan, Röther, Susanne, Reed, Robin, Sträßer, Katja

The TREX (transcription/export) complex couples transcription elongation to the nuclear export of mRNAs. In this article, we show that the poly(A)+ RNA-binding proteins Gbp2 and Hrb1, which resemble...

Functional link between ribosome formation and biogenesis of iron–sulfur proteins

Yarunin, Alexander, Panse, Vikram Govind, Petfalski, Elisabeth, Dez, Christophe, Tollervey, David, Hurt, Ed

In genetic screens for ribosomal export mutants, we identified CFD1, NBP35 and NAR1 as factors involved in ribosome biogenesis. Notably, these components were recently reported to function in...

An intron in the YRA1 gene is required to control Yra1 protein expression and mRNA export in yeast

Rodríguez-Navarro, Susana, Sträßer, Katja, Hurt, Ed

Yra1p is an essential and conserved mRNA export factor in yeast. Strikingly, removal of the intron from YRA1 causes a dominant-negative growth phenotype and a concomitant inhibition of mRNA export....

Recruitment of the human TREX complex to mRNA during splicing

Masuda, Seiji, Das, Rita, Cheng, Hong, Hurt, Ed, Dorman, Nijsje, Reed, Robin

In yeast, the TREX complex contains the THO transcription elongation complex, which functions in direct cotranscriptional recruitment of the mRNA export proteins Sub2 and Yra1 to nascent transcripts....

Formation and nuclear export of tRNA, rRNA and mRNA is regulated by the ubiquitin ligase Rsp5p

Neumann, Silvia, Petfalski, Elisabeth, Brügger, Britta, Großhans, Helge, Wieland, Felix, Tollervey, David, ...

The yeast ubiquitin-protein ligase Rsp5p regulates processes as diverse as polII transcription and endocytosis. Here, we identify Rsp5p in a screen for tRNA export (tex) mutants. The tex23-1/rsp5-3...

The mRNA Export Factor Sus1 Is Involved in Spt/Ada/Gcn5 Acetyltransferase-mediated H2B Deubiquitinylation through Its Interaction with Ubp8 and Sgf11

Köhler, Alwin, Pascual-García, Pau, Llopis, Ana, Zapater, Meritxell, Posas, Francesc, Hurt, Ed, ...

Sus1 acts in nuclear mRNA export via its association with the nuclear pore-associated Sac3–Thp1–Cdc31 complex. In addition, Sus1 plays a role in transcription through its interaction with the...

Nup93, a Vertebrate Homologue of Yeast Nic96p, Forms a Complex with a Novel 205-kDa Protein and Is Required for Correct Nuclear Pore Assembly

Grandi, Paola, Dang, Tam, Pané, Nelly, Shevchenko, Andrej, Mann, Matthias, Forbes, Douglass, ...

Yeast and vertebrate nuclear pores display significant morphological similarity by electron microscopy, but sequence similarity between the respective proteins has been more difficult to observe....

Yeast Ran-Binding Protein 1 (Yrb1) Shuttles between the Nucleus and Cytoplasm and Is Exported from the Nucleus via a CRM1 (XPO1)-Dependent Pathway

Künzler, Markus, Gerstberger, Thomas, Stutz, Françoise, Bischoff, F. Ralf, Hurt, Ed

The RanGTP-binding protein RanBP1, which is located in the cytoplasm, has been implicated in release of nuclear export complexes from the cytoplasmic side of the nuclear pore complex. Here we show...

The Nsp1p Carboxy-Terminal Domain Is Organized into Functionally Distinct Coiled-Coil Regions Required for Assembly of Nucleoporin Subcomplexes and Nucleocytoplasmic Transport

Bailer, Susanne M., Balduf, Carolin, Hurt, Ed

Nucleoporin Nsp1p, which has four predicted coiled-coil regions (coils 1 to 4) in the essential carboxy-terminal domain, is unique in that it is part of two distinct nuclear pore complex (NPC)...

Nuclear Export of 60S Ribosomal Subunits Depends on Xpo1p and Requires a Nuclear Export Sequence-Containing Factor, Nmd3p, That Associates with the Large Subunit Protein Rpl10p

Gadal, Olivier, Strauß, Daniela, Kessl, Jacques, Trumpower, Bernard, Tollervey, David, Hurt, Ed

Nuclear export of ribosomes requires a subset of nucleoporins and the Ran system, but specific transport factors have not been identified. Using a large subunit reporter (Rpl25p-eGFP), we have...

Yeast Los1p Has Properties of an Exportin-Like Nucleocytoplasmic Transport Factor for tRNA

Hellmuth, Klaus, Lau, Denise M., Bischoff, F. Ralf, Künzler, Markus, Hurt, Ed, Simos, George

Saccharomyces cerevisiae Los1p, which is genetically linked to the nuclear pore protein Nsp1p and several tRNA biogenesis factors, was recently grouped into the family of importin/karyopherin-β-like...

Nuclear mRNA Export Requires Complex Formation between Mex67p and Mtr2p at the Nuclear Pores

Santos-Rosa, Helena, Moreno, Horacio, Simos, George, Segref, Alexandra, Fahrenkrog, Birthe, Panté, Nelly, ...

We have identified between Mex67p and Mtr2p a complex which is essential for mRNA export. This complex, either isolated from yeast or assembled in Escherichia coli, can bind in vitro to RNA through...

Cloning and characterization of the Schizosaccharomyces pombe tRNA:pseudouridine synthase Pus1p

Hellmuth, Klaus, Grosjean, Henri, Motorin, Yuri, Deinert, Karina, Hurt, Ed, Simos, George

Saccharomyces cerevisiae cells that carry deletions in both the LOS1 (a tRNA export receptor) and the PUS1 (a tRNA:pseudouridine synthase) genes exhibit a thermosensitive growth defect. A...

A nuclear AAA-type ATPase (Rix7p) is required for biogenesis and nuclear export of 60S ribosomal subunits

Gadal, Olivier, Strauß, Daniela, Braspenning, Joris, Hoepfner, Dominic, Petfalski, Elisabeth, Philippsen, Peter, ...

Ribosomal precursor particles are assembled in the nucleolus before export into the cytoplasm. Using a visual assay for nuclear accumulation of 60S subunits, we have isolated several...

Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins

Lutzmann, Malik, Kunze, Ruth, Buerer, Andrea, Aebi, Ueli, Hurt, Ed

Now that it is likely that all yeast nucleoporins are known, one of the ultimate goals is the in vitro assembly of the entire nuclear pore complex from its ∼30 individual components. Here, we...

60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm

Nissan, Tracy A., Baßler, Jochen, Petfalski, Elisabeth, Tollervey, David, Hurt, Ed

60S ribosomes undergo initial assembly in the nucleolus before export to the cytoplasm and recent analyses have identified several nucleolar pre-60S particles. To unravel the steps in the pathway of...

The mRNA export machinery requires the novel Sac3p–Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores

Fischer, Tamás, Sträßer, Katja, Rácz, Attila, Rodriguez-Navarro, Susana, Oppizzi, Marisa, Ihrig, Petra, ...

Yra1p and Sub2p are components of the TREX complex, which couples transcription elongation with nuclear export of mRNAs. Here, we report a genetic interaction between Yra1p and a conserved protein...

The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes

Schäfer, Thorsten, Strauß, Daniela, Petfalski, Elisabeth, Tollervey, David, Hurt, Ed

Recent reports have increased our knowledge of the consecutive steps during 60S ribosome biogenesis substantially, but 40S subunit formation is less well understood. Here, we investigate the...

Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export

Sträßer, Katja, Hurt, Ed

Mex67p and Mtr2p constitute an essential mRNA export complex that interacts with poly(A)+ RNA and nuclear pore proteins. We have identified Yra1p, an intranuclear protein with in vitro RNA–RNA...

An aminoacylation-dependent nuclear tRNA export pathway in yeast

Grosshans, Helge, Hurt, Ed, Simos, George

Yeast Los1p, the homolog of human exportin-t, mediates nuclear export of tRNA. Using fluorescence in situ hybridization, we could show that the export of some intronless tRNA species is not...

Cotranscriptional recruitment of the serine-arginine-rich (SR)-like proteins Gbp2 and Hrb1 to nascent mRNA via the TREX complex

Hurt, Ed, Luo, Ming-juan, Röther, Susanne, Reed, Robin, Sträßer, Katja

The TREX (transcription/export) complex couples transcription elongation to the nuclear export of mRNAs. In this article, we show that the poly(A)+ RNA-binding proteins Gbp2 and Hrb1, which resemble...

Functional link between ribosome formation and biogenesis of iron–sulfur proteins

Yarunin, Alexander, Panse, Vikram Govind, Petfalski, Elisabeth, Dez, Christophe, Tollervey, David, Hurt, Ed

In genetic screens for ribosomal export mutants, we identified CFD1, NBP35 and NAR1 as factors involved in ribosome biogenesis. Notably, these components were recently reported to function in...

An intron in the YRA1 gene is required to control Yra1 protein expression and mRNA export in yeast

Rodríguez-Navarro, Susana, Sträßer, Katja, Hurt, Ed

Yra1p is an essential and conserved mRNA export factor in yeast. Strikingly, removal of the intron from YRA1 causes a dominant-negative growth phenotype and a concomitant inhibition of mRNA export....

Recruitment of the human TREX complex to mRNA during splicing

Masuda, Seiji, Das, Rita, Cheng, Hong, Hurt, Ed, Dorman, Nijsje, Reed, Robin

In yeast, the TREX complex contains the THO transcription elongation complex, which functions in direct cotranscriptional recruitment of the mRNA export proteins Sub2 and Yra1 to nascent transcripts....

Formation and nuclear export of tRNA, rRNA and mRNA is regulated by the ubiquitin ligase Rsp5p

Neumann, Silvia, Petfalski, Elisabeth, Brügger, Britta, Großhans, Helge, Wieland, Felix, Tollervey, David, ...

The yeast ubiquitin-protein ligase Rsp5p regulates processes as diverse as polII transcription and endocytosis. Here, we identify Rsp5p in a screen for tRNA export (tex) mutants. The tex23-1/rsp5-3...

The mRNA Export Factor Sus1 Is Involved in Spt/Ada/Gcn5 Acetyltransferase-mediated H2B Deubiquitinylation through Its Interaction with Ubp8 and Sgf11

Köhler, Alwin, Pascual-García, Pau, Llopis, Ana, Zapater, Meritxell, Posas, Francesc, Hurt, Ed, ...

Sus1 acts in nuclear mRNA export via its association with the nuclear pore-associated Sac3–Thp1–Cdc31 complex. In addition, Sus1 plays a role in transcription through its interaction with the...

TOR regulates late steps of ribosome maturation in the nucleoplasm via Nog1 in response to nutrients

Honma, Yoshimi, Kitamura, Aiko, Shioda, Ryo, Maruyama, Hironori, Ozaki, Kanako, Oda, Yoko, ...

The protein kinase TOR (target of rapamycin) controls several steps of ribosome biogenesis, including gene expression of rRNA and ribosomal proteins, and processing of the 35S rRNA precursor, in the...

A Novel In Vivo Assay Reveals Inhibition of Ribosomal Nuclear Export in Ran-Cycle and Nucleoporin Mutants

Hurt, Ed, Hannus, Stefan, Schmelzl, Birgit, Lau, Denise, Tollervey, David, Simos, George

To identify components involved in the nuclear export of ribosomes in yeast, we developed an in vivo assay exploiting a green fluorescent protein (GFP)-tagged version of ribosomal protein L25. After...

Rlp7p is associated with 60S preribosomes, restricted to the granular component of the nucleolus, and required for pre-rRNA processing

Gadal, Olivier, Strauss, Daniela, Petfalski, Elisabeth, Gleizes, Pierre-Emmanuel, Gas, Nicole, Tollervey, David, ...

Many analyses have examined subnucleolar structures in eukaryotic cells, but the relationship between morphological structures, pre-rRNA processing, and ribosomal particle assembly has remained...

Structure and Assembly of the Nup84p Complex

Siniossoglou, Symeon, Lutzmann, Malik, Santos-Rosa, Helena, Leonard, Kevin, Mueller, Shirley, Aebi, Ueli, ...

The Nup84p complex consists of five nucleoporins (Nup84p, Nup85p, Nup120p, Nup145p-C, and Seh1p) and Sec13p, a bona fide subunit of the COPII coat complex. We show that a pool of green fluorescent...

Binding of the Mex67p/Mtr2p Heterodimer to Fxfg, Glfg, and Fg Repeat Nucleoporins Is Essential for Nuclear mRNA Export

Sträßer, Katja, Baßler, Jochen, Hurt, Ed

It is not known how Mex67p and Mtr2p, which form a heterodimer essential for mRNA export, transport mRNPs through the nuclear pore. Here, we show that the Mex67p/Mtr2p complex binds to all of the...

Biogenesis of the Signal Recognition Particle (Srp) Involves Import of Srp Proteins into the Nucleolus, Assembly with the Srp-Rna, and Xpo1p-Mediated Export

Grosshans, Helge, Deinert, Karina, Hurt, Ed, Simos, George

The signal recognition particle (SRP) targets nascent secretory proteins to the ER, but how and where the SRP assembles is largely unknown. Here we analyze the biogenesis of yeast SRP, which consists...

The AAA ATPase Rix7 powers progression of ribosome biogenesis by stripping Nsa1 from pre-60S particles

Kressler, Dieter, Roser, Daniela, Pertschy, Brigitte, Hurt, Ed

Ribosome biogenesis takes place successively in the nucleolar, nucleoplasmic, and cytoplasmic compartments. Numerous nonribosomal factors transiently associate with the nascent ribosomes, but the...

A versatile interaction platform on the Mex67–Mtr2 receptor creates an overlap between mRNA and ribosome export

Yao, Wei, Lutzmann, Malik, Hurt, Ed

The transport receptor Mex67–Mtr2 functions in mRNA export, and also by a loop-confined surface on the heterodimer binds to and exports pre-60S particles. We show that Mex67–Mtr2 through the same...

An Endoribonuclease Functionally Linked to Perinuclear mRNP Quality Control Associates with the Nuclear Pore Complexes

Skružný, Michal, Schneider, Claudia, Rácz, Attila, Weng, Julan, Tollervey, David, Hurt, Ed

Nuclear mRNA export is a crucial step in eukaryotic gene expression, which is in yeast coupled to cotranscriptional messenger ribonucleoprotein particle (mRNP) assembly and surveillance. Several...

Membrane curvature induced by Arf1-GTP is essential for vesicle formation

Beck, Rainer, Sun, Zhe, Adolf, Frank, Rutz, Chistoph, Bassler, Jochen, Wild, Klemens, ...

The GTPase Arf1 is considered as a molecular switch that regulates binding and release of coat proteins that polymerize on membranes to form transport vesicles. Here, we show that Arf1-GTP induces...

The inner nuclear membrane protein Src1 associates with subtelomeric genes and alters their regulated gene expression

Grund, Stefanie E., Fischer, Tamás, Cabal, Ghislain G., Antúnez, Oreto, Pérez-Ortín, José E., Hurt, Ed

Inner nuclear membrane proteins containing a LEM (LAP2, emerin, and MAN1) domain participate in different processes, including chromatin organization, gene expression, and nuclear envelope...

Nucleus-Specific and Cell Cycle-Regulated Degradation of Mitogen-Activated Protein Kinase Scaffold Protein Ste5 Contributes to the Control of Signaling Competence▿

Garrenton, Lindsay S., Braunwarth, Andreas, Irniger, Stefan, Hurt, Ed, Künzler, Markus, Thorner, Jeremy

Saccharomyces cerevisiae cells are capable of responding to mating pheromone only prior to their exit from the G1 phase of the cell cycle. Ste5 scaffold protein is essential for pheromone response...

Sus1, Cdc31, and the Sac3 CID Region Form a Conserved Interaction Platform that Promotes Nuclear Pore Association and mRNA Export

Jani, Divyang, Lutz, Sheila, Marshall, Neil J., Fischer, Tamás, Köhler, Alwin, Ellisdon, Andrew M., ...

The yeast Sac3:Cdc31:Sus1:Thp1 (TREX-2) complex facilitates the repositioning and association of actively transcribing genes with nuclear pores (NPCs)—“gene gating”—that is central to...

Sem1 is a functional component of the nuclear pore complex–associated messenger RNA export machinery

Faza, Marius Boulos, Kemmler, Stefan, Jimeno, Sonia, González-Aguilera, Cristina, Aguilera, Andrés, Hurt, Ed, ...

The evolutionarily conserved protein Sem1/Dss1 is a subunit of the regulatory particle (RP) of the proteasome, and, in mammalian cells, binds the tumor suppressor protein BRCA2. Here, we describe a...

Two structurally distinct domains of the nucleoporin Nup170 cooperate to tether a subset of nucleoporins to nuclear pores

Flemming, Dirk, Sarges, Phillip, Stelter, Philipp, Hellwig, Andrea, Böttcher, Bettina, Hurt, Ed

How individual nucleoporins (Nups) perform their role in nuclear pore structure and function is largely unknown. In this study, we examined the structure of purified Nup170 to obtain clues about its...