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Journal Article

Disaggregases in 4 dimensions

MPS-Authors
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Barends,  Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Werbeck,  Nicolas D.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons94928

Reinstein,  Jochen
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://www.sciencedirect.com/science/article/pii/S0959440X09002024/pdfft?md5=2ee5cdbdd2d4c7f50e649bfff43cb223&pid=1-s2.0-S0959440X09002024-main.pdf
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http://dx.doi.org/10.1016/j.sbi.2009.12.014
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Citation

Barends, T., Werbeck, N. D., & Reinstein, J. (2010). Disaggregases in 4 dimensions. Current Opinion in Structural Biology, 20(1), 46-53. doi:10.1016/j.sbi.2009.12.014.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-1FBD-5
Abstract
Non-destructive dissagregation of protein aggregates is a formidable task mediated by the specialized AAA+ chaperone Hsp104/ClpB in combination with the Hsp70/DnaK chaperone system. The exact mechanism of how the hexameric Hsp104/ClpB proteins perform the task of protein disaggregation or remodeling is largely unknown. The process is ATP-dependent and tight coupling between the ATPase domains within the hexameric ring-complex could be observed. While substrate translocation through the central pore of the ring-shaped hexamer appears to be a central mechanism shared with other AAA+ proteins, a middle domain unique to Hsp104/ClpB could be involved in specific features of the Hsp/ClpB mechanism and its regulation. Recent findings underline the dynamic properties of the molecular complex and might provide a basis to understand substrate interaction, regulation of disaggregation activity, and interactions with co-chaperones.