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Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone

Author

Listed:
  • Bryan D. Ryder

    (University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

  • Irina Matlahov

    (University of Pittsburgh School of Medicine
    University of Groningen)

  • Sofia Bali

    (University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

  • Jaime Vaquer-Alicea

    (University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

  • Patrick C. A. Wel

    (University of Pittsburgh School of Medicine
    University of Groningen)

  • Lukasz A. Joachimiak

    (University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

Abstract

The Hsp40/Hsp70 chaperone families combine versatile folding capacity with high substrate specificity, which is mainly facilitated by Hsp40s. The structure and function of many Hsp40s remain poorly understood, particularly oligomeric Hsp40s that suppress protein aggregation. Here, we used a combination of biochemical and structural approaches to shed light on the domain interactions of the Hsp40 DnaJB8, and how they may influence recruitment of partner Hsp70s. We identify an interaction between the J-Domain (JD) and C-terminal domain (CTD) of DnaJB8 that sequesters the JD surface, preventing Hsp70 interaction. We propose a model for DnaJB8-Hsp70 recruitment, whereby the JD-CTD interaction of DnaJB8 acts as a reversible switch that can control the binding of Hsp70. These findings suggest that the evolutionarily conserved CTD of DnaJB8 is a regulatory element of chaperone activity in the proteostasis network.

Suggested Citation

  • Bryan D. Ryder & Irina Matlahov & Sofia Bali & Jaime Vaquer-Alicea & Patrick C. A. Wel & Lukasz A. Joachimiak, 2021. "Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21147-x
    DOI: 10.1038/s41467-021-21147-x
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