Aggregate reactivation mediated by the Hsp100 chaperones

作者：Zolkiewski Michal^*; Zhang Ting; Nagy Maria

来源：Archives of Biochemistry and Biophysics, 2012, 520(1): 1-6.

DOI：10.1016/j.abb.2012.01.012

• Protein aggregation
• Aggregate reactivation
• Molecular chaperone
• ClpB
• Hsp104
• AAA plus ATPase

Hsp100 family of molecular chaperones shows a unique capability to resolubilize and reactivate aggregated proteins. The Hsp100-mediated protein disaggregation is linked to the activity of other chaperones from the Hsp70 and Hsp40 families. The best-studied members of the Hsp100 family are the bacterial ClpB and Hsp104 from yeast. Hsp100 chaperones are members of a large super-family of energy-driven conformational %26quot;machines%26quot; known as AAA+ ATPases. This review describes the current mechanistic model of the chaperone-induced protein disaggregation and explains how the structural architecture of Hsp100 supports disaggregation and how the co-chaperones may participate in the Hsp100-mediated reactions.

• 出版日期2012-4-1