EMD-2332
Structural insights into the chaperone activity of Hsp40: DnaJ binds and remodels RepE
EMD-2332
Single-particle19.0 Å
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Map released: 24/04/2013
Last modified: 25/12/2013
Sample Organism:
Escherichia coli
Sample: DnaJ:RepE complex
Deposition Authors: Cuellar J
,
Perales-Calvo J,
Muga A
,
Valpuesta JM
,
Moro F
Sample: DnaJ:RepE complex
Deposition Authors: Cuellar J
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Structural insights into the chaperone activity of the 40-kDa heat shock protein DnaJ: binding and remodeling of a native substrate.
Cuellar J
,
Perales-Calvo J,
Muga A
,
Valpuesta JM
,
Moro F
(2013) J. Biol. Chem. , 288 , 15065 - 15074
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(2013) J. Biol. Chem. , 288 , 15065 - 15074
Abstract:
Hsp40 chaperones bind and transfer substrate proteins to Hsp70s and regulate their ATPase activity. The interaction of Hsp40s with native proteins modifies their structure and function. A good model for this function is DnaJ, the bacterial Hsp40 that interacts with RepE, the repressor/activator of plasmid F replication, and together with DnaK regulates its function. We characterize here the structure of the DnaJ-RepE complex by electron microscopy, the first described structure of a complex between an Hsp40 and a client protein. The comparison of the complexes of DnaJ with two RepE mutants reveals an intrinsic plasticity of the DnaJ dimer that allows the chaperone to adapt to different substrates. We also show that DnaJ induces conformational changes in dimeric RepE, which increase the intermonomeric distance and remodel both RepE domains enhancing its affinity for DNA.
Hsp40 chaperones bind and transfer substrate proteins to Hsp70s and regulate their ATPase activity. The interaction of Hsp40s with native proteins modifies their structure and function. A good model for this function is DnaJ, the bacterial Hsp40 that interacts with RepE, the repressor/activator of plasmid F replication, and together with DnaK regulates its function. We characterize here the structure of the DnaJ-RepE complex by electron microscopy, the first described structure of a complex between an Hsp40 and a client protein. The comparison of the complexes of DnaJ with two RepE mutants reveals an intrinsic plasticity of the DnaJ dimer that allows the chaperone to adapt to different substrates. We also show that DnaJ induces conformational changes in dimeric RepE, which increase the intermonomeric distance and remodel both RepE domains enhancing its affinity for DNA.