Chaperoned protein disaggregation--the ClpB ring uses its central channel

Arthur L Horwich

doi:10.1016/j.cell.2004.11.018

Chaperoned protein disaggregation--the ClpB ring uses its central channel

Cell. 2004 Nov 24;119(5):579-81. doi: 10.1016/j.cell.2004.11.018.

Author

Arthur L Horwich¹

Affiliation

¹ Howard Hughes Medical Institute and Department of Genetics, Yale University School of Medicine, New Haven, CT 06536 USA.

PMID: 15550237
DOI: 10.1016/j.cell.2004.11.018

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.

Publication types

Review
Comment

MeSH terms

Adenosine Triphosphate / metabolism
Endopeptidase Clp
Escherichia coli Proteins / metabolism*
Heat-Shock Proteins / metabolism*
Heat-Shock Response / physiology
Models, Molecular
Molecular Chaperones / metabolism*
Multiprotein Complexes / metabolism
Protein Subunits / physiology

Substances

Escherichia coli Proteins
Heat-Shock Proteins
Molecular Chaperones
Multiprotein Complexes
Protein Subunits
Adenosine Triphosphate
Endopeptidase Clp
ClpB protein, E coli