PMID: 8955310Dec 1, 1996Paper

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

Journal of Bacteriology
M MontroneWolfgang Marwan

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.

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Citations

Mar 4, 2020·Proceedings of the National Academy of Sciences of the United States of America·Jingyun YangPushkar P Lele
Mar 14, 2008·The EMBO Journal·Galit N Cohen-Ben-LuluMichael Eisenbach
Jun 6, 1998·Proceedings of the National Academy of Sciences of the United States of America·R RamakrishnanR B Bourret
Jun 10, 2004·Microbiology and Molecular Biology Reviews : MMBR·Hendrik Szurmant, George W Ordal
Aug 30, 2002·Applied and Environmental Microbiology·Jung-Kul LeeSang-Yong Kim
Mar 12, 1998·Journal of Bacteriology·M D MansonR M Macnab
Feb 19, 1998·Microbiology·Yehudit Jeziore-SassoonJudith P Armitage
Oct 16, 2003·Genome Research·Torsten NutschErnst Dieter Gilles
Mar 29, 2011·Phytochemistry·Wagner L AraújoAlisdair R Fernie

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