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Structural and dynamical basis for the interaction of HSP70-EEVD with JDP Sis1

View ORCID ProfileCarolina O. Matos, View ORCID ProfileGlaucia M.S. Pinheiro, View ORCID ProfileIcaro P. Caruso, View ORCID ProfileGisele C. Amorim, View ORCID ProfileFabio C. L. Almeida, View ORCID ProfileCarlos H. I. Ramos
doi: https://doi.org/10.1101/2022.11.26.517237
Carolina O. Matos
1Institute of Chemistry, University of Campinas UNICAMP, Campinas SP, Brazil
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Glaucia M.S. Pinheiro
1Institute of Chemistry, University of Campinas UNICAMP, Campinas SP, Brazil
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Icaro P. Caruso
2Multiuser Center for Biomolecular Innovation (CMIB), Department of Physics, São Paulo State University (UNESP), São Jose do Rio Preto, São Paulo, Brazil
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Gisele C. Amorim
3National Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil
4Multidisciplinary Center for Research in Biology (NUMPEX), Campus Duque de Caxias Federal University of Rio de Janeiro, Duque de Caxias, Brazil
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Fabio C. L. Almeida
3National Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil
5National Institute of Science and Technology for Bioimage and Structural Biology INBEB, Brazil
6Institute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil
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  • For correspondence: falmeida@bioqmed.ufrj.br cramos@unicamp.br
Carlos H. I. Ramos
1Institute of Chemistry, University of Campinas UNICAMP, Campinas SP, Brazil
6Institute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil
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  • For correspondence: falmeida@bioqmed.ufrj.br cramos@unicamp.br
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Abstract

Protein folding, refolding and disaggregation are facilitated by the binding and releasing activity of HSP70 proteins. Such activity is aided by J-domain proteins (JDPs, DNAJs or HSP40s) that stimulate the ATPase activity of HSP70 and stabilize complexes between HSP70 and nonnative proteins. The C-terminus EEVD motif of HSP70 interacts with client proteins and with JDPs. Deletion of the EEVD disrupts the ability of HSP70 to associate with class B JDPs. A new understanding of the EEVD interaction with a JDP arises from the results of this work, which gives a detailed NMR characterization of the dynamics and interaction between a class B JDP, Sis1, and the HSP70-EEVD. The EEVD motif binds to multiple sites in Sis1. The interactions at CTDI contribute to the anchoring of HSP70 to Sis1, at site I, and the displacement of the client protein at site II. The competing interaction between the J-domain and the N-terminal boundary of α-helix 6 (at the GF-region) contributes to the interaction of J-domain to HSP70. These results support a mechanism involved in the regulation of the interaction with HSP70 that is autoinhibitory. Finally, a detailed model of the interaction of the EEVD with the J-domain of Sis1 is proposed.

Competing Interest Statement

The authors have declared no competing interest.

  • Abbreviations

    CSP
    chemical shift perturbation
    CTD
    C-Terminal Domain
    HSP
    heat shock protein
    HSP70
    70 kDa heat shock protein
    IDR
    intrinsically disordered region
    JDP
    J-domain protein
    NBD
    nucleotide-binding domain
    R1
    longitudinal relaxation rate
    PRE
    Paramagnetic relaxation enhancement
    R2
    transverse relaxation rate
    SBD
    substrate binding domain
    RMSD
    root-mean-square deviation
    Sis1
    type B JDP from Saccharomyces cerevisiae
    Ssa1
    HSP70 from Saccharomyces cerevisiae;
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    Posted November 26, 2022.
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    Structural and dynamical basis for the interaction of HSP70-EEVD with JDP Sis1
    Carolina O. Matos, Glaucia M.S. Pinheiro, Icaro P. Caruso, Gisele C. Amorim, Fabio C. L. Almeida, Carlos H. I. Ramos
    bioRxiv 2022.11.26.517237; doi: https://doi.org/10.1101/2022.11.26.517237
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    Structural and dynamical basis for the interaction of HSP70-EEVD with JDP Sis1
    Carolina O. Matos, Glaucia M.S. Pinheiro, Icaro P. Caruso, Gisele C. Amorim, Fabio C. L. Almeida, Carlos H. I. Ramos
    bioRxiv 2022.11.26.517237; doi: https://doi.org/10.1101/2022.11.26.517237

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