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Cell Biology and Toxicology

, Volume 22, Issue 1, pp 29–37 | Cite as

Why does ethanol induce cellular heat-shock response?

  • S. Chaudhuri
  • B. Jana
  • T. Basu
Article

Abstract

At the time of induction of the periplasmic protein alkaline phosphatase (AP) in Escherichia coli, the presence of ethanol (10% v/v) in the growth medium did not allow the induced AP to be translocated out to the periplasm. The nontransported AP was stored in the cytoplasm as the unfolded precursor form (AP with its amino-terminal signal sequence), which had no enzymatic activity. The presence of 10% v/v ethanol in the growth medium also induced the heat-shock response in E. coli, which was evident from the enhanced syntheses of several heat-shock proteins (HSPs) over their cellular basal levels. These results, in conjunction with our earlier findings on the occurrence of heat-shock response in an AP-signal sequence mutant of E. coli due to the export deficiency of AP precursor, suggest that the membrane protein precursors, stored in the cytoplasm due to the ethanol-mediated inhibition of translocation, behaved to the cells as abnormal proteins, which ultimately triggered the signal for the induction of heat-shock response in E. coli.

Keywords

Escherichia coli membrane protein translocation heat shock response alkaline phosphatase ethanol 

Abbreviations:

AP

alkaline phosphatase

DTT

dithiothreitol

HRP

horeseradish peroxidose

HSP

heat-shock protein

MOPS

-morpholinpropanesulfonic acid

PAGE

polyacrylamide gel elctrophoresis

PMF

proton-motive force

SDS

sodium docecyl sulfate

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Copyright information

© Springer Science + Business Media, Inc. 2006

Authors and Affiliations

  1. 1.Department of Biochemistry and BiophysicsUniversity of KalyaniKalyaniIndia
  2. 2.Department of Biochemistry and BiophysicsUniversity of KalyaniKalyaniIndia

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