Extended Data Fig. 7: Removal of the HSP70 EEVD tail abolishes binding to class B JDPs.
From: HSP40 proteins use class-specific regulation to drive HSP70 functional diversity
a, b, 1H–13C HMQC spectra of HSP70 (pink) and HSP70(ΔEEVD) (black) showing the isoleucine (a) and valine (b) spectral regions. No conformational changes were detected in the HSP70 chaperone upon deletion of the four C-terminal residues (EEVD). The only visible difference between the two spectra is the lack of the V645 peak in b, as this residue is part of the C-terminal tail that was deleted in HSP70ΔEEVD. c, d, Interaction of HSP70(ΔEEVD) with DNAJA2 (c) and DNAJB1 (d). The interaction between DNAJA2 and HSP70(ΔEEVD) occurs via the same residues as between DNAJA2 and wild-type HSP70 (c, blue; compare to Extended Data Fig. 5c), whereas no interaction was detected between HSP70(ΔEEVD) and DNAJB1 (d, red).
