ClpB dynamics is driven by its ATPase cycle and regulated by the DnaK system and substrate proteins

• DOI: 10.1042/bj20141390
• Publication Date: 2015-01-08T10:36:30Z
• Authors: Alejandra Aguado; José Angel Fernán...; Yovana Cabrera; Fernando Moro; Arturo Muga
• Keywords: CLPB; Random hexamer; Chaperone (clinical); AAA proteins

The hexameric AAA+ (ATPase associated with various cellular activities) chaperone ClpB reactivates protein aggregates in collaboration the DnaK system. An intriguing aspect of function is that active hexamer unstable and therefore questions how this uses multiple rounds ATP hydrolysis to translocate substrates through its central channel. In present paper, we report use biochemical fluorescence tools explore dynamics under different experimental conditions. analysis activity kinetics subunit exchange between hexamers labelled at domains indicates, contrast current view, (i) favours assembly ADP dissociation assembly, (ii) least one order magnitude slower than rate, (iii) are related processes, (iv) substrate proteins regulate ATPase ClpB. These data suggest remain during several events required partially or completely channel, tuned by proteins.