Chaperoned protein disaggregation--the ClpB ring uses its central channel.
In this issue of Cell, exploit a clever manipulation of the Hsp100 ring chaperone, ClpB, to gain some mechanistic and physiologic understanding of the action of this chaperone in mediating ATP-dependent disaggregation of protein aggregates that accumulate in the bacterial cytoplasm under severe heat shock conditions.
Horwich
Arthur L
AL
Howard Hughes Medical Institute and Department of Genetics, Yale University School of Medicine, New Haven, CT 06536 USA.
D000255:Adenosine Triphosphate / Q000378:metabolism; D049071:Endopeptidase Clp; D029968:Escherichia coli Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D018869:Heat-Shock Response / Q000502:physiology; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism*; D046912:Multiprotein Complexes / Q000378:metabolism; D021122:Protein Subunits / Q000502:physiology
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D046912:Multiprotein Complexes; D021122:Protein Subunits; D000255:Adenosine Triphosphate; D049071:Endopeptidase Clp; C069775:ClpB protein, E coli