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Co-translational assembly orchestrates competing biogenesis pathways.

Maximilian Seidel1,2, Anja Becker1, Filipa Pereira3,4

  • 1Department of Molecular Sociology, Max Planck Institute of Biophysics, Frankfurt, Germany.

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|March 10, 2022
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Summary
This summary is machine-generated.

This study reveals how specific protein structural motifs enable co-translational assembly, a process where protein subunits assemble during their synthesis. Researchers identified novel interactions, highlighting the complex regulation of protein complex formation.

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Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling
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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Co-translational assembly, where synthesized protein subunits interact with nascent chains, is crucial for efficient protein complex formation.
  • The precise physiological roles and mechanisms of co-translational assembly, particularly involving nucleoporins, are not fully understood.

Purpose of the Study:

  • To investigate structural motifs in nucleoporins that facilitate co-translational assembly.
  • To identify and characterize novel co-translational interactions.
  • To explore the role of specific motifs in the assembly of multi-complex proteins (moonlighters) and their paralogs.

Main Methods:

  • Examination of structural motifs within nucleoporins.
  • Experimental testing of candidate structural motifs for co-translational assembly potential.
  • Selective ribosome profiling to identify co-translational assembly domains.

Main Results:

  • Several previously unrecognized co-translational interactions were identified.
  • Domain invasion motifs, including beta-propellers, coiled-coils, and short linear motifs, were shown to function as co-translational assembly domains.
  • Proteins involved in multiple complexes (moonlighters) and their paralogs exhibit co-translational assembly in specific, but not all, biogenesis pathways.

Conclusions:

  • Specific structural motifs, such as domain invasion motifs, play a significant role in facilitating co-translational assembly.
  • The assembly of moonlighters and paralogs via co-translational mechanisms is regulated, indicating pathway-specific control.
  • These findings underscore the intricate regulatory mechanisms governing protein complex biogenesis.