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DnaK Chaperone-dependent Disaggregation by Caseinolytic Peptidase B (ClpB) Mutants Reveals Functional Overlap in the N-terminal Domain and Nucleotide-binding Domain-1 Pore Tyrosine

Protein disaggregation in Escherichia coli is carried out by ClpB, an AAA(+) (ATPases associated with various cellular activities) molecular chaperone, together with the DnaK chaperone system. Conformational changes in ClpB driven by ATP binding and hydrolysis promote substrate binding, unfolding, a...

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Wedi'i Gadw mewn:
Manylion Llyfryddiaeth
Prif Awduron: Doyle, Shannon M., Hoskins, Joel R., Wickner, Sue
Fformat: Artigo
Iaith:Inglês
Cyhoeddwyd: American Society for Biochemistry and Molecular Biology 2012
Pynciau:
Mynediad Ar-lein:https://ncbi.nlm.nih.gov/pmc/articles/PMC3436547/
https://ncbi.nlm.nih.gov/pubmed/22745126
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M112.383091
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