Analysis of the conserved acidic residues in the regulatory domain of PhoB

The PhoB protein from Escherichia coli is a member of the two-component signal transduction pathway that controls an adaptive response to limiting phosphate. Activation involves its phosphorylation on a conserved aspartate. Site-directed mutations were introduced at conserved acidic residues. The E9...

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Bibliographic Details
Published inFEBS letters Vol. 441; no. 2; pp. 242 - 246
Main Authors Zundel, Cara J., Capener, Dale C., McCleary, William R.
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 18.12.1998
Subjects
Aspartate phosphorylation
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Base Sequence
DNA Primers
Escherichia coli
Escherichia coli - metabolism
Hydrogen-Ion Concentration
Magnesium - metabolism
Magnesium binding
Mutagenesis, Site-Directed
PhoB
Phosphorylation
Protein Binding
Response regulator
Signal transduction
Spectrometry, Fluorescence
Aspartate phosphorylation
Response regulator
Signal transduction
Escherichia coli
PhoB
Magnesium binding
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Summary:The PhoB protein from Escherichia coli is a member of the two-component signal transduction pathway that controls an adaptive response to limiting phosphate. Activation involves its phosphorylation on a conserved aspartate. Site-directed mutations were introduced at conserved acidic residues. The E9D, D10E, D10N, E11A, E11D and E11Q mutants were each able to induce alkaline phosphatase under low phosphate growth conditions whereas the E9A, D10A, D53A, D53E and D53N could not. The E9Q mutant was constitutively active. Phosphorylation assays showed that only the E9D, E11A, E11Q and E11D mutants were phosphorylated by acetyl phosphate. Most mutants also displayed defects in magnesium binding.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(98)01556-7