Jochen Baßler

article

A Puzzle of Life: Crafting Ribosomal Subunits

Dieter Kressler, Ed Hurt, Jochen Baßler

Trends in Biochemical Sciences > 2017 > 42 > 8 > 640-654

The biogenesis of eukaryotic ribosomes is a complicated process during which the transcription, modification, folding, and processing of the rRNA is coupled with the ordered assembly of ∼80 ribosomal proteins (r-proteins). Ribosome synthesis is catalyzed and coordinated by more than 200 biogenesis factors as the preribosomal subunits acquire maturity on their path from the nucleolus to the cytoplasm...

article

Interaction network of the ribosome assembly machinery from a eukaryotic thermophile

Jochen Baßler, Yasar Luqman Ahmed, Martina Kallas, Markus Kornprobst, more

Protein Science > 26 > 2 > 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 the ribosomal RNA and incorporating ribosomal proteins. Biochemical approaches allowed the isolation and characterization of pre‐ribosomal particles from...

article

The Exosome Is Recruited to RNA Substrates through Specific Adaptor Proteins

Matthias Thoms, Emma Thomson, Jochen Baßler, Marén Gnädig, more

Cell > 2015 > 162 > 5 > 1029-1038

The 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 proteins that recruit the exosome-associated helicase, Mtr4, to unique RNA substrates. Nop53, the yeast homolog of the tumor suppressor PICT1, targets Mtr4 to pre-ribosomal...

article

Einblicke in die Kinderstube der Ribosomen

Jochen Baßler, Ed Hurt

BIOspektrum > 2015 > 21 > 2 > 144-147

Ribosome formation can be imagined like an assembly line for automobile production. Pre-ribosomes transit through a number of ‘mounting-stages’. These different steps are catalyzed by about 200 assembly factors that bind transiently to the evolving ribosome. However, it currently remains unclear how this myriad of factors can trigger ribosome synthesis. Insight into the mechanism of ribosome biogenesis...

article

The power of AAA-ATPases on the road of pre-60S ribosome maturation — Molecular machines that strip pre-ribosomal particles

Dieter Kressler, Ed Hurt, Helmut Bergler, Jochen Baßler

BBA - Molecular Cell Research > 2012 > 1823 > 1 > 92-100

The biogenesis of ribosomes is a fundamental cellular process, which provides the molecular machines that synthesize all cellular proteins. The assembly of eukaryotic ribosomes is a highly complex multi-step process that requires more than 200 ribosome biogenesis factors, which mediate a broad spectrum of maturation reactions. The participation of many energy-consuming enzymes (e.g. AAA-type ATPases,...

article

The AAA-ATPase Rea1 Drives Removal of Biogenesis Factors during Multiple Stages of 60S Ribosome Assembly

Jochen Baßler, Martina Kallas, Brigitte Pertschy, Cornelia Ulbrich, more

Molecular Cell > 2010 > 38 > 5 > 712-721

The AAA ⁺ -ATPase Rea1 removes the ribosome biogenesis factor Rsa4 from pre-60S ribosomal subunits in the nucleoplasm to drive nuclear export of the subunit. To do this, Rea1 utilizes a MIDAS domain to bind a conserved motif in Rsa4. Here, we show that the Rea1 MIDAS domain binds another pre-60S factor, Ytm1, via a related motif. In vivo Rea1 contacts Ytm1 before it contacts Rsa4, and its...

article

Mechanochemical Removal of Ribosome Biogenesis Factors from Nascent 60S Ribosomal Subunits

Cornelia Ulbrich, Meikel Diepholz, Jochen Baßler, Dieter Kressler, more

Cell > 2009 > 138 > 5 > 911-922

The dynein-related AAA ATPase Rea1 is a preribosomal factor that triggers an unknown maturation step in 60S subunit biogenesis. Using electron microscopy, we show that Rea1's motor domain is docked to the pre-60S particle and its tail-like structure, harboring a metal ion-dependent adhesion site (MIDAS), protrudes from the preribosome. Typically, integrins utilize a MIDAS to bind extracellular ligands,...

article

Arx1 Functions as an Unorthodox Nuclear Export Receptor for the 60S Preribosomal Subunit

Bettina Bradatsch, Jun Katahira, Eva Kowalinski, Gert Bange, more

Molecular Cell > 2007 > 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 unconventional export receptor. Arx1 binds directly to FG nucleoporins and exhibits facilitated translocation through NPCs. Moreover, Arx1 functionally...

article

Nuclear Export of Ribosomal 60S Subunits by the General mRNA Export Receptor Mex67-Mtr2

Wei Yao, Daniela Roser, Alwin Köhler, Bettina Bradatsch, more

Molecular Cell > 2007 > 26 > 1 > 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 export of the ribosomal 60S subunit. Biochemical and genetic studies reveal a previously unrecognized interaction surface on the NTF2-like scaffold of the...

article

90S Pre-Ribosomes Include the 35S Pre-rRNA, the U3 snoRNP, and 40S Subunit Processing Factors but Predominantly Lack 60S Synthesis Factors

Paola Grandi, Vladimir Rybin, Jochen Baßler, Elisabeth Petfalski, more

Molecular Cell > 2002 > 10 > 1 > 105-115

We report the characterization of early pre-ribosomal particles. Twelve TAP-tagged components each showed nucleolar localization, sedimented at approximately 90S on sucrose gradients, and coprecipitated both the 35S pre-rRNA and the U3 snoRNA. Thirty-five non-ribosomal proteins were coprecipitated, including proteins associated with U3 (Nop56p, Nop58p, Sof1p, Rrp9, Dhr1p, Imp3p, Imp4p, and Mpp10p)...

article

Identification of a 60S Preribosomal Particle that Is Closely Linked to Nuclear Export

Jochen Baßler, Paola Grandi, Olivier Gadal, Torben Leßmann, more

Molecular Cell > 2001 > 8 > 3 > 517-529

A nuclear GTPase, Nug1p, was identified in a genetic screen for components linked to 60S ribosomal subunit export. Nug1p cosedimented with nuclear 60S preribosomes and was required for subunit export to the cytoplasm. Tagged Nug1p coprecipitated with proteins of the 60S subunit, late precursors to the 25S and 5.8S rRNAs, and at least 21 nonribosomal proteins. These included a homologous nuclear GTPase,...

INFONA - science communication portal

Search results for: Jochen Baßler

A Puzzle of Life: Crafting Ribosomal Subunits

Interaction network of the ribosome assembly machinery from a eukaryotic thermophile

The Exosome Is Recruited to RNA Substrates through Specific Adaptor Proteins

Einblicke in die Kinderstube der Ribosomen

The power of AAA-ATPases on the road of pre-60S ribosome maturation — Molecular machines that strip pre-ribosomal particles

The AAA-ATPase Rea1 Drives Removal of Biogenesis Factors during Multiple Stages of 60S Ribosome Assembly

Mechanochemical Removal of Ribosome Biogenesis Factors from Nascent 60S Ribosomal Subunits

Arx1 Functions as an Unorthodox Nuclear Export Receptor for the 60S Preribosomal Subunit

Nuclear Export of Ribosomal 60S Subunits by the General mRNA Export Receptor Mex67-Mtr2

90S Pre-Ribosomes Include the 35S Pre-rRNA, the U3 snoRNP, and 40S Subunit Processing Factors but Predominantly Lack 60S Synthesis Factors

Identification of a 60S Preribosomal Particle that Is Closely Linked to Nuclear Export

Filter options

Publication date

Publication language

Keywords

Data set

Journal

INFONA - science communication portal

Search results for: Jochen Baßler

Add recipient

Sending message cancelled

Are you sure you want to cancel sending this message?

Send message

Filter options

Publication date

Date range setting

Set the date range to filter the displayed results. You can set a starting date, ending date or both. You can enter the dates manually or choose them from the calendar.

Publication language

Keywords

Data set

Journal

Reporting an error / abuse

Sending the report failed

Accessibility options