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Protein phosphorylation is involved in bacterial chemotaxis

Hess, J. Fred and Oosawa, Kenji and Matsumura, Philip and Simon, Melvin I. (1987) Protein phosphorylation is involved in bacterial chemotaxis. Proceedings of the National Academy of Sciences of the United States of America, 84 (21). pp. 7609-7613. ISSN 0027-8424. PMCID PMC299349. doi:10.1073/pnas.84.21.7609.

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The nature of the biochemical signal that is involved in the excitation response in bacterial chemotaxis is not known. However, ATP is required for chemotaxis. We have purified all of the proteins involved in signal transduction and show that the product of the cheA gene is rapidly autophosphorylated, while some mutant CheA proteins cannot be phosphorylated. The presence of stoichiometric levels of two other purified components in the chemotaxis system, the CheY and CheZ proteins, induces dephosphorylation. We suggest that the phosphorylation of CheA by ATP plays a central role in signal transduction in chemotaxis.

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Additional Information:© 1987 by the National Academy of Sciences. Contributed by Melvin I. Simon, July 22, 1987. This work was supported by Grant AI19296-05 from the National Institutes of Health. Dr. Fred Hess is supported by a Damon Runyon-Walter Winchell Cancer Fund Fellowship, DRG-915. The work in Dr. Philip Matsumura's laboratory is supported by Grant AI18985 from the National Institutes of Health. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Funding AgencyGrant Number
Damon Runyon Cancer Research FoundationDRG-915
Subject Keywords:signal transduction; chemotaxis proteins; ATP; mutagenesis
Issue or Number:21
PubMed Central ID:PMC299349
Record Number:CaltechAUTHORS:HESpnas87
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:7743
Deposited By: Tony Diaz
Deposited On:31 Jul 2007
Last Modified:08 Nov 2021 20:45

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