The transmembrane domains of the sensor kinase KdpD of Escherichia coli are not essential for sensing K+ limitation.

Abstract:

:The sensor kinase/response regulator system KdpD/KdpE of Escherichia coli regulates the expression of the kdpFABC operon, which encodes the high affinity K+ transport system KdpFABC. The membrane-bound sensor kinase KdpD consists of four transmembrane domains, a large cytoplasmic N-terminal domain and a cytoplasmic C-terminal transmitter domain. To elucidate the role of the four transmembrane domains, various deletions were introduced in kdpD and the activities of the resulting truncated derivatives of KdpD were determined. A KdpD protein lacking all four transmembrane domains was able to sense low K+ concentrations, whereas at higher K+ concentrations kdpFABC expression was constitutive. These and further results with various truncated KdpD proteins lacking distinct parts of the transmembrane domains or derivatives in which a linker peptide or two transmembrane domains of PutP, the Na+/proline transporter of Escherichia coli, replaced the missing part indicated that the transmembrane domains are not essential for sensing of K+ limitation, but may be important for the correct positioning of the large N- and C-terminal cytoplasmic domains to each other.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Heermann R,Fohrmann A,Altendorf K,Jung K

doi

10.1046/j.1365-2958.2003.03348.x

subject

Has Abstract

pub_date

2003-02-01 00:00:00

pages

839-48

issue

3

eissn

0950-382X

issn

1365-2958

pii

3348

journal_volume

47

pub_type

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