Seeing protein unfolding and degradation by an archaeal proteolytic machinery by fluorescence-coupled real-time SANS
A tightly regulated proteome (i.e. the ensemble of proteins in a cell) is of paramount importance throughout the life cycle of any biological cell. An important step, apart from transcriptional and translational control mechanism, is proteolysis, i.e. the controlled degradation of proteins. A major key player in this mechanism is the proteasome and a dysfunction of proteolysis can have severe impact on cells and lead to health problems or death in humans. In the present proposal we build on a previous real-time SANS project that has studied the dynamics of an isolated proteasome partner, the archaeal PAN unfoldase complex, and its activity on a tagged GFP substrate. Now, we propose to widen this study by including the crucial 20S proteasome partner in solution. By combining SANS with online fluorescence spectroscopy (to follow the unfolding of GFP) and temperature activation, we expect to gain unprecedented insights into the kinetics of protein unfolding in solution and into the concomitant conformational changes of PAN at a time resolution of about 30 seconds.
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GABEL Frank; FRANZETTI Bruno; HOGREL Gaelle; MAHIEU Emilie and MARTEL Anne. (2017). Seeing protein unfolding and degradation by an archaeal proteolytic machinery by fluorescence-coupled real-time SANS. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-904
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