Catching protein unfolding by AAA+ ATPases in the act: a SANS study of an intermediate unfolding state of GFP
The specific recognition, unfolding and degradation of faulty proteins is an essential process in any living cell in order to guarantee protein homeostasis and keep the proteome in a healthy and functional state. Dysfunction of this process can lead to accumulation of misfolded proteins that are potentially toxic and lead to multiple diseases. Despite the crucial importance of understanding this process, detailed structural insights, at a molecular level, are limited, mainly due to specific flexibility and conformational changes involved. Here, we propose to study the intermediate unfolded state of a specifically tagged model protein, GFPssrA-biotin/avidin, by SANS in solution. The presence of a biotin/avidin-tag will allow to block GFP within the unfoldase complex PAN. Using alternate deuteration of either partner will allow us to both describe the specific conformation of GFP and PAN during the process. In addition, an online fluorescence device on D22 will monitor the folded state of GFP. By arresting the unfoldase/substrate complex, the structural interpretation/analysis can be much more advanced and detailed than in a previous pioneering study carried out at ILL.
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GABEL Frank; FRANZETTI Bruno; MAHIEU Emilie and MARTEL Anne. (2018). Catching protein unfolding by AAA+ ATPases in the act: a SANS study of an intermediate unfolding state of GFP. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-927
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