title: The specificity of fumarate as a switching factor of the bacterial flagellar motor.
abstract: Fumarate restores to flagella of cytoplasm-free, Che Y-containing envelopes of Escherichia coli and Salmonella typhimurium the ability to switch from one direction of rotation to another. To examine the specificity of this effect, we studied flagellar rotation of envelopes which contained, instead of fumarate, one of its analogues. Malate, maleate and succinate promoted switching, but to a lesser extent than fumarate. These observations were made both with wild-type envelopes and with envelopes of a mutant which lacks the enzymes succinate dehydrogenase and fumarase, indicating that the switching-promoting activity of the analogues was not caused by their conversion to fumarate. Aspartate and lactate did not promote switching. Using strains defective in specific enzymes of the tricarboxylic acid cycle and lacking the cytoplasmic chemotaxis proteins as well as some of the chemotaxis receptors, we demonstrated that, in intact bacteria, unlike the situation in envelopes, fumarate promoted clockwise rotation via its metabolites acetyl phosphate and acetyladenylate, but did not promote switching (presumably because of the presence of cytoplasmic fumarate). All of the results are consistent with the notion that fumarate acts as a switching factor, presumably by lowering the activation energy of switching. Thus fumarate and some of its metabolites may serve as a connection point between the bacterial metabolic state and chemotactic behaviour.
authors.affiliation: Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot, Israel.
authors.forename: R
authors.initials: R
authors.lastname: Barak
authors.forename: I
authors.initials: I
authors.lastname: Giebel
authors.forename: M
authors.initials: M
authors.lastname: Eisenbach
mesh_terms: D001224:Aspartic Acid / Q000378:metabolism / Q000494:pharmacology; D001426:Bacterial Proteins / Q000494:pharmacology; D002633:Chemotaxis / Q000235:genetics; D004926:Escherichia coli / Q000378:metabolism*; D005407:Flagella / Q000378:metabolism*; D005650:Fumarates / Q000378:metabolism / Q000494:pharmacology*; D019344:Lactic Acid / Q000378:metabolism / Q000494:pharmacology; D008293:Malates / Q000378:metabolism / Q000494:pharmacology; D008298:Maleates / Q000378:metabolism / Q000494:pharmacology; D008565:Membrane Proteins / Q000494:pharmacology; D000072236:Methyl-Accepting Chemotaxis Proteins; D012399:Rotation; D012486:Salmonella typhimurium / Q000235:genetics*; D013386:Succinates / Q000378:metabolism / Q000494:pharmacology; D019802:Succinic Acid
chemical_list: D001426:Bacterial Proteins; D005650:Fumarates; D008293:Malates; D008298:Maleates; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D013386:Succinates; D001224:Aspartic Acid; D019344:Lactic Acid; C030298:malic acid; C032005:fumaric acid; C030272:maleic acid; D019802:Succinic Acid