Domain stability in the AAA+ ATPase ClpB from Escherichia coli.

Archives of Biochemistry and Biophysics
Maria NagyMichal Zolkiewski

Abstract

ClpB is a heat-shock protein that reactivates aggregated proteins in cooperation with the DnaK chaperone system. ClpB belongs to the family of AAA+ ATPases and forms ring-shaped oligomers: heptamers in the absence of nucleotides and hexamers in the presence of nucleotides. We investigated the thermodynamic stability of ClpB in its monomeric and oligomeric forms. ClpB contains six distinct structural domains: the N-terminal domain involved in substrate binding, two AAA+ ATP-binding modules, each consisting of two domains, and a coiled-coil domain inserted between the AAA+ modules. We produced seven variants of ClpB, each containing a single Trp located in each of the ClpB domains and measured the changes in Trp fluorescence during the equilibrium urea-induced unfolding of ClpB. We found that two structural domains: the small domain of the C-terminal AAA+ module and the coiled-coil domain were destabilized in the oligomeric form of ClpB, which indicates that only those domains change their conformation and/or interactions during formation of the ClpB rings.

References

Jul 13, 2000·The Journal of Cell Biology·R D Vale
Jul 28, 2001·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·T Ogura, A J Wilkinson
Dec 4, 2003·Biochemistry·Sabina KedzierskaMichal Zolkiewski

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Citations

Aug 9, 2020·Frontiers in Microbiology·Mingzhu HuangXuelan Chen
Nov 15, 2020·The Journal of Biological Chemistry·Przemyslaw GlazaMichal Zolkiewski
Dec 6, 2018·International Journal of Biological Macromolecules·Anindya BiswasSubrata Sau

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