Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock.

doi:10.1016/j.abb.2007.04.006

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Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock.

Archives of biochemistry and biophysics - 1 Aug 2007

Skorko-Glonek Joanna, Laskowska Ewa, Sobiecka-Szkatula Anna, Lipinska Barbara

Abstract excerpt

The protective action of chaperone-like activity of HtrA protease against protein aggregation was studied. High levels of proteolytically inactive HtrAS210A (active center serine replaced by alanine) suppressed the temperature-sensitive phenotype of the htrA mutants. The ability of HtrAS210A to alleviate the lethality of htrA bacteria at high temperatures correlated well with the observed decrease of cellular...

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Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock.

Abstract excerpt

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Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock.

Abstract excerpt

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