Phosphorylation-independent bacterial chemoresponses correlate with changes in the cytoplasmic level of fumarate.

Abstract:

:Bacterial chemotaxis is based on modulation of the probability to switch the direction of flagellar rotation. Responses to many stimuli are transduced by a two-component system via reversible phosphorylation of CheY, a small cytoplasmic protein that directly interacts with the switch complex at the flagellar motor. We found that the chemorepellents indole and benzoate induce motor switching in Escherichia coli cells with a disabled phosphorylation cascade. This phosphorylation-independent chemoresponse is explained by reversible inhibition of fumarase by indole or benzoate which leads to an increased level of cellular fumarate, a compound involved in motor switching for bacteria and archaea. Genetic deletion of fumarase increased the intracellular concentration of fumarate and enhanced the switching frequency of the flagellar motors irrespective of the presence or absence of the phosphorylation cascade. These correlations provide evidence for fumarate-dependent metabolic signal transduction in bacterial chemosensing.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Montrone M,Oesterhelt D,Marwan W

doi

10.1128/jb.178.23.6882-6887.1996

subject

Has Abstract

pub_date

1996-12-01 00:00:00

pages

6882-7

issue

23

eissn

0021-9193

issn

1098-5530

journal_volume

178

pub_type

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