Role of the DnaK-ClpB bichaperone system in DNA gyrase reactivation during a severe heat-shock response in Escherichia coli.

Abstract

In Escherichia coli cells, an increase in temperature induces immediate DNA relaxation, followed by the fast recovery of DNA supercoiling. DNA gyrase, proteins synthesized during heat stress, and chaperone DnaK have been proposed to participate in this recovery. However, the mechanism of DNA supercoiling recovery has not been completely elucidated. The results presented here suggest that in cells exposed to severe heat-shock stress, DNA supercoiling levels are recovered by the reactivation of DNA gyrase. This reactivation involves solubilization of a fraction of protein GyrA present in protein aggregates, by the bichaperone DnaK-ClpB system.

• Authors: Teresa Lara-Ortíz, Juan Castro-Dorantes, Jesús Ramírez-Santos, M Carmen Gómez-Eichelmann
• Journal: Canadian journal of microbiology (Can J Microbiol) Vol. 58 Issue 2 Pg. 195-9 (Feb 2012) ISSN: 1480-3275 [Electronic] Canada
• PMID: 22263929 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• DNA, Superhelical
• Escherichia coli Proteins
• HSP70 Heat-Shock Proteins
• Heat-Shock Proteins
• Molecular Chaperones
• Endopeptidase Clp
• ClpB protein, E coli
• DNA Gyrase

Topics

• DNA Gyrase (metabolism)
• DNA, Superhelical (metabolism)
• Endopeptidase Clp
• Escherichia coli (genetics, metabolism, physiology)
• Escherichia coli Proteins (genetics, metabolism)
• HSP70 Heat-Shock Proteins (genetics, metabolism)
• Heat-Shock Proteins (genetics, metabolism)
• Heat-Shock Response (physiology)
• Molecular Chaperones (genetics, metabolism)