Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Bettina Bradatsch"'
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 23, p 9108 (2020)
The ribosome assembly factor Nsa2 is part of the Rea1-Rsa4-Nsa2 interconnected relay on nuclear pre-60S particles that is essential for 60S ribosome biogenesis. Cryo-EM structures depict Nsa2 docked via its C-terminal β-barrel domain to nuclear pre-
Externí odkaz:
https://doaj.org/article/8c17172b141340d8afff238bde9a436a
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 9108, p 9108 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 23
International Journal of Molecular Sciences
Volume 21
Issue 23
The ribosome assembly factor Nsa2 is part of the Rea1-Rsa4-Nsa2 interconnected relay on nuclear pre-60S particles that is essential for 60S ribosome biogenesis. Cryo-EM structures depict Nsa2 docked via its C-terminal &beta
barrel domain to nucl
barrel domain to nucl
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
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
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
Autor:
Reiner Peters, Wei Yao, Yoshihiro Yoneda, Toshihiro Sekimoto, Gert Bange, Klemens Wild, Bettina Bradatsch, Jun Katahira, Ed Hurt, Irmi Sinning, Guido Boese, Viola Baumgärtel, Eva Kowalinski, Jochen Bassler
Publikováno v:
Molecular Cell. 27(5):767-779
Shuttling transport receptors carry cargo through nuclear pore complexes (NPCs) via transient interactions with Phe-Gly (FG)-rich nucleoporins. Here, we identify Arx1, a factor associated with a late 60S preribosomal particle in the nucleus, as an un
Publikováno v:
Molecular Cell. 26:51-62
The yeast Mex67-Mtr2 complex and its homologous metazoan counterpart TAP-p15 operate as nuclear export receptors by binding and translocating mRNA through the nuclear pore complexes. Here, we show how Mex67-Mtr2 can also function in the nuclear expor
Autor:
Gert Bange, Christoph Leidig, Roland Beckmann, Matthias Thoms, Bettina Bradatsch, Iris Holdermann, Ed Hurt, Irmgard Sinning, Otto Berninghausen
Publikováno v:
Nature communications. 5
During eukaryotic ribosome biogenesis, nascent ribosomal RNA (rRNA) forms pre-ribosomal particles containing ribosomal proteins and assembly factors. Subsequently, these immature rRNAs are processed and remodelled. Little is known about the premature
Autor:
Gert Bange, Stefan Amlacher, Yoshihiro Yoneda, Irmgard Sinning, Bettina Bradatsch, Jun Katahira, Yutaka Ogawa, Dagmar Pratte, Dieter Kressler, Ed Hurt, Goran Stjepanovic, Daniela Strauß
Publikováno v:
Science (New York, N.Y.). 338(6107)
Symportin Synchrony Ribosomes, the macromolecular machines responsible for protein synthesis, function in the cytoplasm but are assembled in the nucleus. Ribosomal proteins must be imported into the nucleus, but how this is coordinated with assembly
Autor:
Gerald N. Rechberger, Ed Hurt, Jochen Baßler, Bettina Bradatsch, Martina Kallas, Maria Anna Wagner, Isabella Klein, Claudia Schmidt, Heimo Strohmaier, Emma Thomson, Helmut Bergler
Publikováno v:
Molecular and cellular biology. 32(24)
The nuclear export of the preribosomal 60S (pre-60S) subunit is coordinated with late steps in ribosome assembly. Here, we show that Bud20, a conserved C(2)H(2)-type zinc finger protein, is an unrecognized shuttling factor required for the efficient
Autor:
Sebastian Falk, Stefan Amlacher, Gert Bange, Manimozhiyan Arumugam, Daniel R. Mende, Peer Bork, Vera van Noort, Ed Hurt, Irmgard Sinning, Christopher J. Creevey, Bettina Bradatsch
Publikováno v:
'BMC Evolutionary Biology ', vol: 13, pages: 7-1-7-13 (2013)
BMC Evolutionary Biology, Vol 13, Iss 1, p 7 (2013)
BMC Evolutionary Biology
BMC Evolutionary Biology, Vol 13, Iss 1, p 7 (2013)
BMC Evolutionary Biology
Background Proteomes of thermophilic prokaryotes have been instrumental in structural biology and successfully exploited in biotechnology, however many proteins required for eukaryotic cell function are absent from bacteria or archaea. With Chaetomiu