Výsledky vyhledávání - "Marén Gnädig"

Interaction network of the ribosome assembly machinery from a eukaryotic thermophile

Autor: Markus Kornprobst, Matthias Thoms, Satyavati Kharde, Ed Hurt, Bettina Bradatsch, Sherif Ismail, Martina Kallas, Gunter Stier, Dirk Flemming, Yasar Luqman Ahmed, Marén Gnädig, Irmgard Sinning, Jochen Baßler, Nestor Castillo, Sabine Griesel, Emma Thomson, Sonja Bastuck, Fabiola R. Calviño

Publikováno v: Protein Science. 26:327-342

Ribosome biogenesis in eukaryotic cells is a highly dynamic and complex process innately linked to cell proliferation. The assembly of ribosomes is driven by a myriad of biogenesis factors that shape pre-ribosomal particles by processing and folding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b5c8e0dcbedd809e196aa7d4c08921e0
https://doi.org/10.1002/pro.3085

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The Exosome Is Recruited to RNA Substrates through Specific Adaptor Proteins

Autor: Matthias Thoms, Sabine Griesel, Marén Gnädig, Emma Thomson, Ed Hurt, Jochen Baßler

Publikováno v: Cell. 162:1029-1038

SummaryThe exosome regulates the processing, degradation, and surveillance of a plethora of RNA species. However, little is known about how the exosome recognizes and is recruited to its diverse substrates. We report the identification of adaptor pro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae941418d7f32bd865e9f9682b1061bc
https://doi.org/10.1016/j.cell.2015.07.060

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Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel

Autor: Bettina Bradatsch, Bettina Böttcher, Sander Granneman, David Tollervey, Ed Hurt, Christoph Leidig, Roland Beckmann, Marén Gnädig

Publikováno v: Nature structural & molecular biology
Bradatsch, B, Leidig, C, Granneman, S, Gnädig, M, Tollervey, D, Böttcher, B, Beckmann, R & Hurt, E 2012, ' Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel ', Nature Structural & Molecular Biology . https://doi.org/10.1038/nsmb.2438

Pre-ribosomal particles evolve in the nucleus through transient interaction with biogenesis factors, before export to the cytoplasm. Here, we report the architecture of the late pre-60S particle purified from Saccharomyces cerevisiae through Arx1, a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dedb30b2e357ad4effa295a559293759
http://europepmc.org/articles/PMC3678077

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RNA Helicase Prp43 and Its Co-factor Pfa1 Promote 20 to 18 S rRNA Processing Catalyzed by the Endonuclease Nob1

Autor: Thorsten Schäfer, David Tollervey, Marén Gnädig, Ed Hurt, Brigitte Pertschy, Claudia Schneider

Publikováno v: Journal of Biological Chemistry. 284:35079-35091

Many RNA nucleases and helicases participate in ribosome biogenesis, but how they cooperate with each other is largely unknown. Here we report that in vivo cleavage of the yeast pre-rRNA at site D, the 3'-end of the 18 S rRNA, requires functional int

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea9cb75e60c00fddc7587146e4083e9d
https://doi.org/10.1074/jbc.m109.040774

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Formation and Nuclear Export of Preribosomes Are Functionally Linked to the Small-Ubiquitin-Related Modifier Pathway

Autor: Dieter Kressler, Marén Gnädig, Vikram Govind Panse, David Tollervey, Ed Hurt, Andrea Pauli, Elisabeth Petfalski

Publikováno v: Traffic

Ribosomal precursor particles are initially assembled in the nucleolus prior to their transfer to the nucleoplasm and export to the cytoplasm. In a screen to identify thermosensitive (ts) mutants defective in the export of pre-60S ribosomal subunit,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff31cfcb1ea8dbf98e44e937cd4f1551
https://europepmc.org/articles/PMC7610852/