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

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

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...

Université de Fribourg

Sequential domain assembly of ribosomal protein S3 drives 40S subunit maturation

Mitterer, Valentin ; Murat, Guillaume ; Réty, Stéphane ; Blaud, Magali ; Delbos, Lila ; Stanborough, Tamsyn ; Bergler, Helmut ; Leulliot, Nicolas ; Kressler, Dieter ; Pertschy, Brigitte

In: Nature Communications, 2016, vol. 7, p. 10336

Eukaryotic ribosomes assemble by association of ribosomal RNA with ribosomal proteins into nuclear precursor particles, which undergo a complex maturation pathway coordinated by non-ribosomal assembly factors. Here, we provide functional insights into how successive structural re-arrangements in ribosomal protein S3 promote maturation of the 40S ribosomal subunit. We show that S3 dimerizes...

Université de Fribourg

Yar1 protects the ribosomal protein rps3 from aggregation

Koch, Barbara ; Mitterer, Valentin ; Niederhauser, Johannes ; Stanborough, Tamsyn ; Murat, Guillaume ; Rechberger, Gerald ; Bergler, Helmut ; Kressler, Dieter ; Pertschy, Brigitte

In: The journal of Biological Chemistry, 2012, p. -

2000 ribosomes have to be synthesized in yeast every minute. Therefore the fast production of ribosomal proteins, their efficient delivery to the nucleus and correct incorporation into ribosomal subunits are prerequisites for optimal growth rates. Here, we report that the ankyrin repeat protein Yar1 directly interacts with the small ribosomal subunit protein Rps3 and accompanies newly synthesized...