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Volumn 274, Issue 5286, 1996, Pages 423-425

Signaling by the Escherichia coli aspartate chemoreceptor tar with a single cytoplasmic domain per dimer

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; DIMER; MEMBRANE RECEPTOR;

EID: 0029803848     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.274.5286.423     Document Type: Article
Times cited : (68)

References (40)
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    • Tar-A198EΔSfu lacks three-quarters of the signaling region but retains the first three methylation sites (K1 region). Tar-A198EΔKpn completely lacks the signaling region. Tar-A198EΔTth lacks the first two-thirds of the cytoplasmic signaling domain and retains the COOH-terminal 160 residues, including the fourth methylation site (R1 region). Tar-A198EΔNde, Tar-A198EΔBstP, Tar-A198EΔBsrF, and Tar-A198EΔNru lack part of the linker region and all of the signaling domain. When expressed in strain RP4372recA, none of these mutant receptors mediated an aspartate response (Fig. 2).
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    • This strain produces only the ribose-galactose chemoreceptor Trg [F thi thr leu met eda rpsL Δ(tar-tap)5201 tsr-1; A. Boyd, A. Krikos, M. I. Simon, Cell 26, 333 (1981)].
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    • We also examined swarming abilities of the cells in tryptone semisolid agar (0.25%). Many of them swarmed, whereas cells expressing Tar-A198EΔTth, Tar-A198EΔBstP, Tar-A198EΔBsrF, and Tar-A198EΔNru did not. However, even those cells that did not swarm responded to aspartate (Fig. 2).
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    • which lacks all four chemoreceptors, was used as a host, cells coexpressing Tar-A19K and one of the deleted versions of Tar responded to glycerol, whereas cells expressing only Tar-A19K did not respond. Therefore, the Tar-A19K homodimer seems to lack the ability to mediate a glycerol response
    • Cells expressing only Tar-A19K also responded to 1 M glycerol (Fig. 2, A to G). However, when strain HCB339 [A. J. Wolfe, M. P. Conley, T. J. Kramer, H. C. Berg, J. Bacteriol. 169, 1878 (1987)]. which lacks all four chemoreceptors, was used as a host, cells coexpressing Tar-A19K and one of the deleted versions of Tar responded to glycerol, whereas cells expressing only Tar-A19K did not respond. Therefore, the Tar-A19K homodimer seems to lack the ability to mediate a glycerol response.
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    • Similar results were obtained with strain HCB339 as the host, suggesting that Trg is not responsible for the aspartate responses of RP4372recA cells expressing the heterodimers.
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    • 154 is in contact with aspartate is responsible for signal production (16).
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    • discuss possible mechanisms for such indirect interaction
    • P. J. Gardina and M. D. Manson [Science 274, 425 (1996)] discuss possible mechanisms for such indirect interaction.
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    • note
    • We thank M. D. Manson and P. J. Gardina for communicating unpublished results and for helpful discussions. Supported in part by grants-in-aid for scientific research to I.K. from the Ministry of Education, Science, and Culture of Japan.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.