Domain swapping reveals that the N-terminal domain of the sensor kinase KdpD in Escherichia coli is important for signaling |
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Authors: | Ralf Heermann Marie-Luise Lippert Kirsten Jung |
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Institution: | 1. Ludwig-Maximilians-Universit?t München, Biozentrum, Bereich Mikrobiologie, Gro?haderner Str. 2-4, D-82152, Martinsried, Germany 2. Munich Center of integrated Protein Science CiPSM, München, Germany 3. Philipps-Universit?t Marburg, Fachbereich Biologie, Mikrobiologie, Karl-von-Frisch-Str. 8, D-35043, Marburg, Germany
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Abstract: | Background The KdpD/KdpE two-component system of Escherichia coli regulates expression of the kdpFABC operon encoding the high affinity K+ transport system KdpFABC. The input domain of KdpD comprises a domain that belongs to the family of universal stress proteins
(Usp). It has been previously demonstrated that UspC binds to this domain, resulting in KdpD/KdpE scaffolding under salt stress.
However the mechanistic significance of this domain for signaling remains unclear. Here, we employed a "domain swapping" approach
to replace the KdpD-Usp domain with four homologous domains or with the six soluble Usp proteins of E. coli. |
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