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Journal of Bacteriology, February 2003, p. 1112-1115, Vol. 185, No. 3
0021-9193/03/$08.00+0 DOI: 10.1128/JB.185.3.1112-1115.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Genetic and Biochemical Studies of Phosphatase Activity of PhoR
Daniel O. Carmany,
Kristine Hollingsworth,
and William R. McCleary*
Microbiology and Molecular Biology Department, Brigham Young University, Provo, Utah 84602-5253
Received 6 September 2002/
Accepted 30 October 2002
In Escherichia coli, PhoR is the histidine kinase of the phosphate regulon. It has been postulated that PhoR may function as a phospho-PhoB phosphatase. Experiments with four precise phoR deletion mutants supported this hypothesis and suggested that this activity resides within the histidine phosphorylation domain. This biochemical activity was confirmed by using a separately expressed histidine phosphorylation domain.
* Corresponding author. Mailing address: Microbiology and Molecular Biology Department, Brigham Young University, 775 WIDB, Provo, UT 84602-5253. Phone: (801) 422-8793. Fax: (801) 422-0519. E-mail:
bill_mccleary{at}byu.edu.
Present address: Life Science Division, Battelle Dugway Operations, Dugway Proving Ground, UT 84022.
Present address: Austin Community College, Austin, TX 78701.
Journal of Bacteriology, February 2003, p. 1112-1115, Vol. 185, No. 3
0021-9193/03/$08.00+0 DOI: 10.1128/JB.185.3.1112-1115.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
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