Solution structure of the natively assembled yeast ribosomal stalk determined by small-angle X-ray scattering

Author:

Grela Przemysław1,Gajda Michal J.23,Armache Jean-Paul4,Beckmann Roland4,Krokowski Dawid1,Svergun Dmitri I.2,Grankowski Nikodem1,Tchórzewski Marek1

Affiliation:

1. Department of Molecular Biology, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland

2. European Molecular Biology Laboratory, Hamburg Outstation, Notkestrasse 85, 22603 Hamburg, Germany

3. Max-Planck Karl Bonhoeffer Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany

4. Gene Center, Department of Biochemistry, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany

Abstract

The ribosomal stalk of the 60S subunit has been shown to play a crucial role in all steps of protein synthesis, but its structure and exact molecular function remain an unanswered question. In the present study, we show the low-resolution models of the solution structure of the yeast ribosomal stalk, composed of five proteins, P0–(P1–P2)2. The model of the pentameric stalk complex determined by small-angle X-ray scattering reveals an elongated shape with a maximum length of 13 nm. The model displays three distinct lobes, which may correspond to the individual P1–P2 heterodimers anchored to the C-terminal domain of the P0 protein.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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