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A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE

Nature Structural Biology volume 1, pages 95–101 (1994)Cite this article

Abstract

The activity of DnaK (Hsp70) chaperones in assisting protein folding relies on DnaK binding and ATP–controlled release of protein substrates. The ATPase activity of DnaK is tightly controlled by the nucleotide exchange factor GrpE. We find that GrpE interacts stably with the amino–terminal ATPase domain of DnaK. Analysis of the mutant DnaK756 protein, which has a lower affinity for GrpE, reveals a role for residue Gly 32 in GrpE binding. Gly 32 is located in an exposed loop near the nucleotide binding site of DnaK. Deletion of this loop prevents stable GrpE binding, ATPase stimulation by GrpE, and DnaK chaperone activity. Conservation of this loop within the Hsp70 family suggests that cooperation between Hsp70 and GrpE–like proteins may be a general feature of this class of chaperone.

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Author notes

  1. Alexander Buchberger and Hartwig Schröder: A.B. and H.S. contributed equally to this work

Authors and Affiliations

  1. Zentrum für Molekulare Biologie, Universität Heidelberg, INF 282, D69120, Heidelberg, FRG

    Alexander Buchberger, Hartwig Schröder, Martina Büttner & Bernd Bukau

  2. European Molecular Biology Laboratory, Meyerhofstr. 1, D-69117, Heidelberg, FRG

    Alfonso Valencia

Authors
  1. Alexander Buchberger
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  2. Hartwig Schröder
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  3. Martina Büttner
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  4. Alfonso Valencia
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  5. Bernd Bukau
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Buchberger, A., Schröder, H., Büttner, M. et al. A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nat Struct Mol Biol 1, 95–101 (1994). https://doi.org/10.1038/nsb0294-95

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