Molecular mechanism of J-domain-triggered ATP hydrolysis by Hsp70 chaperones
Efficient targeting of Hsp70 chaperones to substrate proteins depends on J-domain cochaperones, which in synergism with substrates trigger ATP hydrolysis in Hsp70s and concomitant substrate trapping. We present the crystal structure of the J-domain of Escherichia coli DnaJ in complex with the E. col...
Gespeichert in:
| Hauptverfasser: | , , |
|---|---|
| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
18 January 2018
|
| In: |
Molecular cell
Year: 2017, Jahrgang: 69, Heft: 2, Pages: 227-237,e1-e4 |
| ISSN: | 1097-4164 |
| Online-Zugang: |
|
| Verfasserangaben: | Roman Kityk, Jürgen Kopp, Matthias P. Mayer |
| Zusammenfassung: | Efficient targeting of Hsp70 chaperones to substrate proteins depends on J-domain cochaperones, which in synergism with substrates trigger ATP hydrolysis in Hsp70s and concomitant substrate trapping. We present the crystal structure of the J-domain of Escherichia coli DnaJ in complex with the E. coli Hsp70 DnaK. The J-domain interacts not only with DnaK's nucleotide-binding domain (NBD) but also with its substrate-binding domain (SBD) and packs against the highly conserved interdomain linker. Mutational replacement of contacts between J-domain and SBD strongly reduces the ability of substrates to stimulate ATP hydrolysis in the presence of DnaJ and compromises viability at heat shock temperatures. Our data demonstrate that the J-domain and the substrate do not deliver completely independent signals for ATP hydrolysis, but the J-domain, in addition to its direct influence on Hsp70s catalytic center, makes Hsp70 more responsive for the hydrolysis-inducing signal of the substrate, resulting in efficient substrate trapping. |
|---|---|
| Beschreibung: | Gesehen am 15.10.2018 Available online 28 December 2017 |
| Beschreibung: | Online Resource |
| ISSN: | 1097-4164 |