Journal of Bacteriology, June 2000, p. 3314-3318, Vol. 182, No. 11
Division of Biological Science, Graduate
School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan
Received 3 January 2000/Accepted 17 March 2000
PomA is thought to be a component of the ion channel in the
sodium-driven polar-flagellar motor of Vibrio
alginolyticus. We have found that some cysteine substitutions in
the periplasmic region of PomA result in a slow-motility phenotype, in
which swarming and swimming speeds are reduced even in the presence of
high concentrations of NaCl. Most of the mutants showed a sodium ion
dependence similar to that of the wild type but with significantly
reduced motility at all sodium ion concentrations. By contrast,
motility of the D31C mutant showed a sharp dependence on NaCl
concentration, with a threshold at 38 mM. The motor of the D31C mutant
rotates stably, as monitored by laser dark-field microscopy, suggesting
that the mutant PomA protein is assembled normally into the motor
complex. Mutational studies of Asp31 suggest that, although this
residue is not essential for motor rotation, a negative charge at this position contributes to optimal speed and/or efficiency of the motor.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
A Slow-Motility Phenotype Caused by Substitutions
at Residue Asp31 in the PomA Channel Component of a Sodium-Driven
Flagellar Motor

*
Corresponding author. Mailing address: Division of
Biological Science, Graduate School of Science, Nagoya University,
Chikusa-ku, Nagoya 464-8602, Japan. Phone: 81-52-789-2991. Fax:
81-52-789-3001. E-mail:
g44416a{at}nucc.cc.nagoya-u.ac.jp.
Present address: Department of Biology, University of Utah, Salt
Lake City, UT 84112.
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