Hsp104 and Potentiated Variants Can Operate as Distinct Nonprocessive Translocases

Heat shock protein (Hsp) 104 is a hexameric ATPases associated with diverse cellular activities motor protein that enables cells to survive extreme stress. Hsp104 couples the energy of ATP binding and hydrolysis to solubilize proteins trapped in aggregated structures. The mechanism by which Hsp104 d...

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Veröffentlicht in:	Biophysical journal 2019-05, Vol.116 (10), p.1856-1872
Hauptverfasser:	Durie, Clarissa L., Lin, JiaBei, Scull, Nathaniel W., Mack, Korrie L., Jackrel, Meredith E., Sweeny, Elizabeth A., Castellano, Laura M., Shorter, James, Lucius, Aaron L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Amino Acid Sequence Heat-Shock Proteins - genetics Heat-Shock Proteins - metabolism Hydrolysis Kinetics Mutant Proteins - metabolism Peptides - metabolism Protein Aggregates Protein Binding Protein Conformation Protein Folding Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Structure-Activity Relationship
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