Chaperoned protein disaggregation--the ClpB ring uses its central channel.
basic_science · Level V
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Abstract
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.
Medical subject headings
- Escherichia coli Proteins
- Heat-Shock Proteins
- Molecular Chaperones