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Chaperone-assisted protein aggregate reactivation: Different solutions for the same problem.

Alejandra Aguado1, José Angel Fernández-Higuero1, Fernando Moro1

  • 1Unidad de Biofísica (CSIC-UPV/EHU) y Departamento de Bioquímica y Biología Molecular, Facultad de Ciencia y Tecnología, Universidad del País Vasco (UPV/EHU), 48080 Bilbao, Spain.

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Oligomeric chaperones like Hsp104 and ClpB reactivate aggregated proteins, crucial for stress survival. This review details their mechanism and the distinct disaggregase systems in animals lacking Hsp100 proteins.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Oligomeric AAA+ chaperones Hsp100 (Hsp104, ClpB) are vital for protein aggregate reactivation in yeast and bacteria.
  • This activity is essential for cell survival under severe stress conditions.
  • Hsp100 proteins are absent in metazoans, which utilize Hsp70 and Hsp110 families for similar functions.

Purpose of the Study:

  • To review the current understanding of Hsp100-mediated protein aggregate reactivation.
  • To elucidate the mechanism of disaggregase activity, including ATP-induced conformational changes and assembly dynamics.
  • To discuss the human disaggregase machinery and the role of Hsp110.

Main Methods:

  • Review of existing literature on Hsp100, Hsp70, Hsp40, and Hsp110 chaperone families.
  • Analysis of ATP-induced conformational changes and oligomeric assembly dynamics.
  • Examination of allosteric coupling within hexameric ring complexes.

Main Results:

  • Hsp100 disaggregase activity is linked to Hsp70 and Hsp40 chaperones.
  • ATP-driven conformational changes and regulated assembly dynamics are key to Hsp100 function.
  • Metazoans employ Hsp70 and Hsp110 systems for protein aggregate disaggregation in the absence of Hsp100.

Conclusions:

  • The precise mechanism of protein aggregate untangling by Hsp100 remains an active area of research.
  • The absence of Hsp100 homologs in metazoans suggests potential as antimicrobial targets.
  • Understanding human disaggregase machinery, particularly Hsp110's role, is crucial for cellular health.