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Journal of Bacteriology, March 2000, p. 1437-1441, Vol. 182, No. 5
Department of Biotechnology, Division of
Utilization of Biological Resources, Faculty of Agriculture, Gifu
University, Gifu 501-1193,1 and Division
of Biological Science, Graduate School of Science, Nagoya
University, Chikusa-ku, Nagoya 464-8602,2 Japan
Received 8 September 1999/Accepted 8 December 1999
The chemoreceptor Tcp mediates taxis to citrate. To identify
citrate-binding residues, we substituted cysteine for seven basic or
polar residues that are chosen based on the comparison of Tcp with the
well-characterized chemoreceptors. The results suggest that Arg-63,
Arg-68, Arg-72, Lys-75, and Tyr-150 (and probably other unidentified
residues) are involved in the recognition of citrate.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Mutational Analysis of Ligand Recognition by Tcp,
the Citrate Chemoreceptor of Salmonella enterica
Serovar Typhimurium

*
Corresponding author. Mailing address: Division of
Biological Science, Graduate School of Science, Nagoya University,
Chikusa-ku, Nagoya 464-8602, Japan. Phone: 81-52-789-2993. Fax:
81-52-789-3001. E-mail:
i45406a{at}nucc.cc.nagoya-u.ac.jp.
Present address: Department of Clinical Pathology, Division of
Molecular Cytogenetics, International Medical Center of Japan, 1-21-1 Toyama, Shinjuku-ku, Tokyo 162-8655, Japan.
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