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Verfasst von:Bi, Shuangyu [VerfasserIn]   i
 Yu, Daqi [VerfasserIn]   i
 Si, Guangwei [VerfasserIn]   i
 Luo, Chunxiong [VerfasserIn]   i
 Li, Tongqing [VerfasserIn]   i
 Ouyang, Qi [VerfasserIn]   i
 Jakovljević, Vladimir [VerfasserIn]   i
 Sourjik, Victor [VerfasserIn]   i
 Tu, Yuhai [VerfasserIn]   i
 Lai, Luhua [VerfasserIn]   i
Titel:Discovery of novel chemoeffectors and rational design of Escherichia coli chemoreceptor specificity
Verf.angabe:Shuangyu Bi, Daqi Yu, Guangwei Si, Chunxiong Luo, Tongqing Li, Qi Ouyang, Vladimir Jakovljevic, Victor Sourjik, Yuhai Tu, and Luhua Lai
E-Jahr:2013
Jahr:September 15, 2013
Umfang:6 S.
Fussnoten:Gesehen am 25.11.2020
Titel Quelle:Enthalten in: National Academy of Sciences (Washington, DC)Proceedings of the National Academy of Sciences of the United States of America
Ort Quelle:Washington, DC : National Acad. of Sciences, 1915
Jahr Quelle:2013
Band/Heft Quelle:110(2013), 42, Seite 16814-16819
ISSN Quelle:1091-6490
Abstract:Bacterial chemoreceptors mediate chemotactic responses to diverse stimuli. Here, by using an integrated in silico, in vitro, and in vivo approach, we screened a large compound library and found eight novel chemoeffectors for the Escherichia coli chemoreceptor Tar. Six of the eight new Tar binding compounds induce attractant responses, and two of them function as antagonists that can bind Tar without inducing downstream signaling. Comparison between the antagonist and attractant binding patterns suggests that the key interactions for chemotaxis signaling are mediated by the hydrogen bonds formed between a donor group in the attractant and the main-chain carbonyls (Y149 and/or Q152) on the α4 helix of Tar. This molecular insight for signaling is verified by converting an antagonist to an attractant when introducing an N-H group into the antagonist to restore the hydrogen bond. Similar signal triggering effect by an O-H group is also confirmed. Our study suggests that the Tar chemoeffector binding pocket may be separated into two functional regions: region I mainly contributes to binding and region II contributes to both binding and signaling. This scenario of binding and signaling suggests that Tar may be rationally designed to respond to a nonnative ligand by altering key residues in region I to strengthen binding with the novel ligand while maintaining the key interactions in region II for signaling. Following this strategy, we have successfully redesigned Tar to respond to l-arginine, a basic amino acid that does not have chemotactic effect for WT Tar, by two site-specific mutations (R69′E and R73′E).
DOI:doi:10.1073/pnas.1306811110
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: https://doi.org/10.1073/pnas.1306811110
 Volltext: https://www.pnas.org/content/110/42/16814
 DOI: https://doi.org/10.1073/pnas.1306811110
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1740991885
Verknüpfungen:→ Zeitschrift

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