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Université de Fribourg

Suppressor mutations in Rpf2–Rrs1 or Rpl5 bypass the Cgr1 function for pre-ribosomal 5S RNP-rotation

Thoms, Matthias ; Mitterer, Valentin ; Kater, Lukas ; Falquet, Laurent ; Beckmann, Roland ; Kressler, Dieter ; Hurt, Ed

In: Nature Communications, 2018, vol. 9, no. 1, p. 4094

During eukaryotic 60S biogenesis, the 5S RNP requires a large rotational movement to achieve its mature position. Cryo-EM of the Rix1-Rea1 pre-60S particle has revealed the post-rotation stage, in which a gently undulating α-helix corresponding to Cgr1 becomes wedged between Rsa4 and the relocated 5S RNP, but the purpose of this insertion was unknown. Here, we show that cgr1 deletion in...

Université de Fribourg

An ATP-dependent partner switch links flagellar C-ring assembly with gene expression

Blagotinsek, Vitan ; Schwan, Meike ; Steinchen, Wieland ; Mrusek, Devid ; Hook, John C. ; Rossmann, Florian ; Freibert, Sven A. ; Kratzat, Hanna ; Murat, Guillaume ; Kressler, Dieter ; Beckmann, Roland ; Beeby, Morgan ; Thormann, Kai M. ; Bange, Gert

In: Proceedings of the National Academy of Sciences, 2020, vol. 117, no. 34, p. 20826–20835

Bacterial flagella differ in their number and spatial arrangement. In many species, the MinD-type ATPase FlhG (also YlxH/FleN) is central to the numerical control of bacterial flagella, and its deletion in polarly flagellated bacteria typically leads to hyperflagellation. The molecular mechanism underlying this numerical control, however, remains enigmatic. Using the model species Shewanella...

Université de Fribourg

Ubiquitin release from eL40 is required for cytoplasmic maturation and function of 60S ribosomal subunits in Saccharomyces cerevisiae

Martín‐Villanueva, Sara ; Fernández‐Pevida, Antonio ; Fernández‐Fernández, José ; Kressler, Dieter ; Cruz, Jesús de la

In: The FEBS Journal, 2019, vol. 0, no. 0, p. -

Ubiquitin is generated by proteolytic cleavage of precursor proteins in which it is fused either to itself, constituting a linear polyubiquitin protein of head‐to‐tail monomers, or as a single N‐terminal moiety to one of two ribosomal proteins, eL40 (Ubi1/2 precursors) and eS31 (Ubi3 precursor). It has been proposed that the ubiquitin moiety fused to these ribosomal proteins could act...

Université de Fribourg

The ubiquitin moiety of ubi1 is required for productive expression of ribosomal protein el40 in saccharomyces cerevisiae

Martín-Villanueva, Sara ; Fernández-Pevida, Antonio ; Kressler, Dieter ; Cruz, Jesús de la

In: Cells, 2019, vol. 8, no. 8, p. 850

Ubiquitin is a highly conserved small eukaryotic protein. It is generated by proteolytic cleavage of precursor proteins in which it is fused either to itself, constituting a polyubiquitin precursor of head-to-tail monomers, or as a single N-terminal moiety to ribosomal proteins. Understanding the role of the ubiquitin fused to ribosomal proteins becomes relevant, as these proteins are...

Université de Fribourg

Conformational proofreading of distant 40S ribosomal subunit maturation events by a long-range communication mechanism

Mitterer, Valentin ; Shayan, Ramtin ; Ferreira-Cerca, Sébastien ; Murat, Guillaume ; Enne, Tanja ; Rinaldi, Dana ; Weigl, Sarah ; Omanic, Hajrija ; Gleizes, Pierre-Emmanuel ; Kressler, Dieter ; Plisson-Chastang, Celia ; Pertschy, Brigitte

In: Nature Communications, 2019, vol. 10, no. 1, p. 2754

Eukaryotic ribosomes are synthesized in a hierarchical process driven by a plethora of assembly factors, but how maturation events at physically distant sites on pre- ribosomes are coordinated is poorly understood. Using functional analyses and cryo- EM, we show that ribosomal protein Rps20 orchestrates communication between two multi-step maturation events across the pre-40S subunit. Our...

Université de Fribourg

Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME

Rössler, Ingrid ; Embacher, Julia ; Pillet, Benjamin ; Murat, Guillaume ; Liesinger, Laura ; Hafner, Jutta ; Unterluggauer, Julia Judith ; Birner-Gruenberger, Ruth ; Kressler, Dieter ; Pertschy, Brigitte

In: Nucleic Acids Research, 2019, p. gkz317

Dedicated chaperones protect newly synthesized ribosomal proteins (r-proteins) from aggregation and accompany them on their way to assembly into nascent ribosomes. Currently, only nine of the ∼80 eukaryotic r-proteins are known to be guarded by such chaperones. In search of new dedicated r-protein chaperones, we performed a tandem-affinity purification based screen and looked for factors...

Université de Fribourg

A puzzle of life: crafting ribosomal subunits

Kressler, Dieter ; Hurt, Ed ; Baßler, Jochen

In: Trends in Biochemical Sciences, 2017, p. -

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...

Université de Fribourg

Hold on to your friends: dedicated chaperones of ribosomal proteins

Pillet, Benjamin ; Mitterer, Valentin ; Kressler, Dieter ; Pertschy, Brigitte

In: BioEssays, 2017, vol. 39, no. 1, p. -

Eukaryotic ribosomes are assembled from their components, the ribosomal RNAs and ribosomal proteins, in a tremendously complex, multi-step process, which primarily takes place in the nuclear compartment. Therefore, most ribosomal proteins have to travel from the cytoplasm to their incorporation site on pre-ribosomes within the nucleus. However, due to their particular characteristics, such as...

Université de Fribourg

Nuclear import of dimerized ribosomal protein Rps3 in complex with its chaperone Yar1

Mitterer, Valentin ; Gantenbein, Nadine ; Birner-Gruenberger, Ruth ; Murat, Guillaume ; Bergler, Helmut ; Kressler, Dieter ; Pertschy, Brigitte

In: Scientific Reports, 2016, vol. 6, p. 36714

After their cytoplasmic synthesis, ribosomal proteins need to be transported into the nucleus, where they assemble with ribosomal RNA into pre-ribosomal particles. Due to their physicochemical properties, they need protection from aggregation on this path. Newly synthesized ribosomal protein Rps3 forms a dimer that is associated with one molecule of its specific chaperone Yar1. Here we report...