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Methods to Classify Cytoplasmic Foci as Mammalian Stress Granules
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Structural insights into stressosome assembly.

Eunju Kwon1, Deepak Pathak1, Han-Ul Kim2

  • 1College of Pharmacy, Yeungnam University, Gyeongsan, Gyeongbuk 38541, Republic of Korea.

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|October 3, 2019
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Summary
This summary is machine-generated.

Bacterial stressosome assembly involves RsbS and RsbR proteins forming a pseudo-icosahedral core. Non-conserved residues in conserved STAS folds dictate how these proteins interact, ensuring bacterial survival under stress.

Keywords:
STAS domainX-ray crystallographycryo-electron microscopycrystal structurepseudo-icosahedronsingle-particle cryo-EMstressosome

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Area of Science:

  • Structural Biology
  • Microbiology
  • Biochemistry

Background:

  • The stressosome is crucial for bacterial survival, transducing environmental stress signals to SigB to regulate gene expression.
  • Its core, composed of RsbS and RsbR proteins, forms a pseudo-icosahedral structure with 60 STAS domains.

Purpose of the Study:

  • To elucidate the assembly mechanism of the bacterial stressosome core.
  • To understand how RsbS and RsbR paralogs interact to form the functional complex.

Main Methods:

  • Utilized crystal structure of RsbS and cryo-electron microscopy (cryo-EM) of RsbRA-RsbS complexes.
  • Applied diverse symmetry restraints (C1, D2, I) to cryo-EM data for structural analysis.
  • Reconstructed a detailed model of the stressosome core based on structural data and mutational analysis.

Main Results:

  • RsbS monomers fit well into an icosahedral cryo-EM structure, indicating a conserved STAS fold with RsbRA.
  • Distinct N-domain protrusions of RsbRA in the C1 envelope allowed differentiation of RsbRA and RsbS STAS domains.
  • Mutational analysis confirmed the role of specific RsbRA residues in RsbS interaction, highlighting their importance in stressosome assembly.

Conclusions:

  • The study presents a refined model for bacterial stressosome core assembly.
  • Conserved STAS folds between RsbS and RsbR proteins are essential, but non-conserved residues within these folds determine specific protein interactions and assembly outcomes.