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- W2912173668 abstract "The unfoldase/disaggregase function of Hsp104 is achieved by ATP binding and hydrolysis. Some single-site mutations of Hsp104 enhance its innate capability of aggregate dissolution and suppression of proteotoxicity of amyloid-forming proteins. Hsp104 function potentiation is frequently associated with faster ATP turnover. Illustration of the mechanism of potentiation requires a better understanding of the Hsp104 ATPase cycle e.g. the identity of the rate limiting step. ADP release has been identified as rating limiting for several protein systems with ATPase activity. Measuring ADP release is however challenging. In particular for Hsp104, there are at least two obstacles i) it has two different AAA (ATPases Associated with diverse cellular Activities) nucleotide binding domains (NBD) both are capable of ATP binding and hydrolysis making just measuring ADP binding affinity ambiguous as a result of averaging between the two NBDs. Moreover, its steady-state ATP hydrolysis rate is in the range of 1s−1 rendering the commonly applied methods of kinetic measurements difficult to implement. Hydrogen-deuterium exchange probes conformational dynamics of protein main-chain amides. By taking advantage of the substantially different HX rates of Walker A motif (the most critical nucleotide binding structure element) with or without ADP bound, we apply a fast HX labeling strategy as a non-perturbing and label-free way to measure the kinetics of ADP binding and release in a NBD-resolved fashion. We’ve found that the ADP off rate of NBD1 matches perfectly with the steady-state ATP hydrolysis rate which mainly takes place in NBD1. We’ve also found that, of two of the most potentiated Hsp104 variants, ie. I187F and A503S, their elevated ATPase turnover can be entirely attributed to faster ADP off from NBD1. In addition, I187F appears to hydrolyze ATP more cooperatively due to a strengthened protomer interface." @default.
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- W2912173668 date "2019-02-01" @default.
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- W2912173668 title "Mechanism of Hsp104 Function Potentiation Studied by Hydrogen-Deuterium Exchange Detected by Mass Spectrometry (HX-Ms)" @default.
- W2912173668 doi "https://doi.org/10.1016/j.bpj.2018.11.2612" @default.
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