Conserved distal loop residues in the HSP104 and CLPB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation

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Abstract

Background: How Hsp104 and ClpB coordinate polypeptide handover with Hsp70 to dissolve disordered protein aggregates is unknown. Results: Conserved distal loop residues in the Hsp104 and ClpB middle domain contact NBD2 and enable Hsp70-dependent protein disaggregation. Conclusion: Distal loop does not project out into solution and Hsp104 and ClpB are tuned differently for Hsp70 collaboration. © 2014 by the American Society for Biochemistry and Molecular Biology, Inc. .

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DeSantis, M. E., Sweeny, E. A., Snead, D., Leung, E. H., Go, M. S., Gupta, K., … Shorter, J. (2014). Conserved distal loop residues in the HSP104 and CLPB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation. Journal of Biological Chemistry, 289(2), 848–867. https://doi.org/10.1074/jbc.M113.520759

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