Extended Data Fig. 5: HSP70 binds to the CTDI of DNAJB1 but not of DNAJA2.
From: HSP40 proteins use class-specific regulation to drive HSP70 functional diversity

a–c, Overlay of 1H–13C HMQC correlation maps of ILVM-labelled HSP70 (black) and HSP70 in complex with DNAJB1 (a, light red), DNAJB1 J-domain (b, dark red), and DNAJB1 CTDs (c, cyan). The DNAJB1 J-domain interacts with residues in the HSP70 nucleotide-binding domain and substrate-binding domain, similar to the interaction observed between E. coli DnaK and the J-domain of DnaJ8. DNAJB1 CTDs, however, interact with a different region of HSP70, corresponding to the disordered C-terminal tail of HSP70. d–f, Interaction of ILVM-labelled HSP70 with DNAJA2 (d, light blue), DNAJA2 J-domain (e, dark blue) and DNAJA2 CTDs (f, green). The residues of the DNAJA2 J-domain interact with similar HSP70 residues to the DNAJB1 J-domain, in both cases located at the interface between the nucleotide-binding domain and the substrate-binding domain. Unlike DNAJB1, however, no interaction was observed between the DNAJA2 CTDs and HSP70.