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Vol. 10, Issue 4, 1133-1146, April 1999
*Department of Physiology and Biophysics, Albert Einstein College
of Medicine, Bronx, New York 10461; Chemotaxis of Escherichia coli toward
phosphotransferase systems (PTSs)-carbohydrates requires
phosphoenolpyruvate-dependent PTSs as well as the chemotaxis response
regulator CheY and its kinase, CheA. Responses initiated by flash
photorelease of a PTS substrates D-glucose and its
nonmetabolizable analog methyl National Institute
for Medical Research, Mill Hill, London NW7 1AA, United Kingdom; and
Fachbereich Biologie/Chemie, Universität
Osnabrück, 49069 Osnabrück, Germany
-D-glucopyranoside were
measured with 33-ms time resolution using computer-assisted motion
analysis. This, together with chemotactic mutants, has allowed us to
map out and characterize the PTS chemotactic signal pathway. The
responses were absent in mutants lacking the general PTS enzymes EI or
HPr, elevated in PTS transport mutants, retarded in mutants lacking
CheZ, a catalyst of CheY autodephosphorylation, and severely reduced in
mutants with impaired methyl-accepting chemotaxis protein (MCP)
signaling activity. Response kinetics were comparable to those
triggered by MCP attractant ligands over most of the response range,
the most rapid being 11.7 ± 3.1 s
1. The response
threshold was <10 nM for glucose. Responses to methyl
-D-glucopyranoside had a higher threshold, commensurate with a lower PTS affinity, but were otherwise kinetically
indistinguishable. These facts provide evidence for a single pathway in
which the PTS chemotactic signal is relayed rapidly to MCP-CheW-CheA
signaling complexes that effect subsequent amplification and slower
CheY dephosphorylation. The high sensitivity indicates that this signal is generated by transport-induced dephosphorylation of the PTS rather
than phosphoenolpyruvate consumption.
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