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Papers In Press, published online ahead of print November 7, 2001
Graduate School of Science, Nagoya University, Nagoya, Aichi prefecture 464-8602
Corresponding Author: i45406a{at}cc.nagoya-u.ac.jp
The two major chemoreceptors of Escherichia coli, Tsr and Tar, mediate opposite responses to the same changes in intracellular pH (pHi). We set out to identify residues involved in pHi sensing to gain insight into the general mechanisms of signaling employed by the chemoreceptors. Characterization of various chimeras of Tsr and Tar localized the pHi-sensing region to Arg259-His267 of Tar and Gly261-Asp269 of Tsr. This region of Tar contains three charged residues (Arg259-Ser261, Asp263 and His267) that have counterparts of opposite charge in Tsr (Gly261-Glu262, Arg265 and Asp269). The replacement of all of the three charged residues in Tar or Arg259-Ser260 alone by the corresponding residues of Tsr reversed the polarity of pHi response, whereas the replacement of Asp263 or His267 did not change the polarity but altered the time course of pHi response. These results suggest that the electrostatic properties of a short cytoplasmic region within the linker region that connects the second transmembrane helix to the first methylation helix is critical for switching the signaling state of the chemoreceptors during pH sensing. Similar conformational changes of this region in response to external ligands may be critical components of transmembrane signaling.
J. Biol. Chem, 10.1074/jbc.M109930200
Submitted on October 15, 2001
Revised on November 6, 2001
Accepted on November 6, 2001
Sensing of cytoplasmic pH by bacterial chemoreceptors involves the linker region that connects the membrane-spanning and the signal-modulating helices
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