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DnaJ recruits DnaK to protein aggregates.

Sergio P Acebrón1, Vanesa Fernández-Sáiz1, Stefka G Taneva1

  • 1Unidad de Biofísica (Consejo Superior de Investigaciones Científicas/Universidad del País Vasco-Euskal Henriko Unibertsitatea) and Departamento de Bioquímica y Biología Molecular, Universidad del País Vasco, P.O. Box 644, Bilbao 48080, Spain.

The Journal of Biological Chemistry
|November 7, 2007
PubMed
Summary

Heat-induced protein aggregates are reactivated by Hsp70 chaperones. This study shows bacterial Hsp70 (DnaK) requires its cochaperone (DnaJ) to bind aggregates, with mutations impairing this process.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Thermal stress causes protein aggregation within cells.
  • Hsp100 and Hsp70 chaperones are crucial for reactivating protein aggregates.
  • DnaK is the bacterial homolog of Hsp70.

Purpose of the Study:

  • To investigate the interaction of bacterial Hsp70 (DnaK) with aggregated protein substrates.
  • To elucidate the role of the cochaperone DnaJ in this interaction.

Main Methods:

  • Studied DnaK's interaction with various aggregated model substrates.
  • Investigated the effect of mutations in DnaK's 'latch' region on DnaJ affinity and chaperone activity.
  • Assessed the impact of varying DnaJ concentrations on mutant DnaK activity.

Main Results:

  • DnaK binding to large protein aggregates is mediated by DnaJ.
  • Mutations in DnaK's 'latch' region reduce DnaJ affinity and impair aggregate removal.
  • Chaperone activity is restored by increasing DnaJ concentration, indicating a threshold for DnaK recruitment.

Conclusions:

  • DnaJ is essential for recruiting DnaK to protein aggregate surfaces.
  • A minimum number of DnaK molecules bound to aggregates is necessary for efficient reactivation.
  • This study provides the first experimental evidence for DnaJ-mediated recruitment of ATP-DnaK to aggregates.