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Related Concept Videos

Ribosomes01:27

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Magnetic bacteria exhibit a directed movement called magnetotaxis, driven by structures called magnetosomes. These magnetosomes consist of chains of magnetic particles made of either magnetite (Fe₃O₄) or greigite (Fe₃S₄) and are organized in a linear conformation by a protein scaffold within invaginations of the cell membrane. The bacteria align along the north–south magnetic field lines, much like a compass needle. They are typically microaerophilic or anaerobic...
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
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Collided ribosomes form a unique structural interface to induce Hel2-driven quality control pathways.

Ken Ikeuchi1, Petr Tesina2, Yoshitaka Matsuo1

  • 1Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.

The EMBO Journal
|January 6, 2019
PubMed
Summary
This summary is machine-generated.

Ribosome stalling activates mRNA (no-go decay) and protein (ribosome-associated quality control) quality control. Hel2-dependent ubiquitination is key for disome-coupled NGD and RQC, while Not4 mediates NGD outside disomes.

Keywords:
RQT complexno‐go mRNA decayribosome collisionribosome quality controlubiquitination

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Ribosome stalling triggers distinct mRNA (no-go decay, NGD) and nascent polypeptide (ribosome-associated quality control, RQC) quality control pathways.
  • In yeast, RQC involves Hel2-dependent uS10 ubiquitination and the RQT complex.

Purpose of the Study:

  • To investigate the roles of Hel2-dependent uS10 ubiquitination and the RQT complex in NGD and RQC within di-ribosome (disome) units.
  • To elucidate the mechanisms of quality control triggered by ribosome collisions.

Main Methods:

  • In vitro translation assays to assess Hel2 ubiquitination activity on monosomes versus disomes.
  • Cryo-electron microscopy (Cryo-EM) to determine the structure of disome units.
  • Reporter mRNA assays to analyze NGD and RQC pathways in the absence of key factors.

Main Results:

  • Hel2 preferentially ubiquitinated disomes over monosomes on a reporter mRNA.
  • Cryo-EM revealed a distinct disome structure recognized by Hel2.
  • Absence of RQT or uS10 ubiquitination abolished disome-specific NGD, leading to alternative Hel2-mediated cleavages.
  • Not4-mediated monoubiquitination of eS7 and subsequent Hel2 polyubiquitination were observed in RQC-uncoupled NGD.

Conclusions:

  • Hel2-mediated ribosome ubiquitination is essential for both canonical NGD (NGDRQC+) and RQC coupled to disomes.
  • RQC-uncoupled NGD (NGDRQC-) occurring outside disomes is dependent on Not4 activity.