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Open Access Research article

The protein interaction network of a taxis signal transduction system in a Halophilic Archaeon

Matthias Schlesner12*, Arthur Miller1, Hüseyin Besir13, Michalis Aivaliotis14, Judith Streif15, Beatrix Scheffer16, Frank Siedler16 and Dieter Oesterhelt1*

Author Affiliations

1 Department of Membrane Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany

2 Division of Theoretical Bioinformatics (B080), German Cancer Research Center (DKFZ), Heidelberg, Germany

3 Protein Expression & Purification Core Facility, EMBL Heidelberg, Germany

4 Institute of Molecular Biology and Biotechnology, FORTH, Heraklion, Crete, Greece

5 Institute of Microbiology, Technische Universität Braunschweig, Braunschweig, Germany

6 Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany

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BMC Microbiology 2012, 12:272  doi:10.1186/1471-2180-12-272

Published: 21 November 2012

Abstract

Background

The taxis signaling system of the extreme halophilic archaeon Halobacterium (Hbt.) salinarum differs in several aspects from its model bacterial counterparts Escherichia coli and Bacillus subtilis. We studied the protein interactions in the Hbt. salinarum taxis signaling system to gain an understanding of its structure, to gain knowledge about its known components and to search for new members.

Results

The interaction analysis revealed that the core signaling proteins are involved in different protein complexes and our data provide evidence for dynamic interchanges between them. Fifteen of the eighteen taxis receptors (halobacterial transducers, Htrs) can be assigned to four different groups depending on their interactions with the core signaling proteins. Only one of these groups, which contains six of the eight Htrs with known signals, shows the composition expected for signaling complexes (receptor, kinase CheA, adaptor CheW, response regulator CheY). From the two Hbt. salinarum CheW proteins, only CheW1 is engaged in signaling complexes with Htrs and CheA, whereas CheW2 interacts with Htrs but not with CheA. CheY connects the core signaling structure to a subnetwork consisting of the two CheF proteins (which build a link to the flagellar apparatus), CheD (the hub of the subnetwork), two CheC complexes and the receptor methylesterase CheB.

Conclusions

Based on our findings, we propose two hypotheses. First, Hbt. salinarum might have the capability to dynamically adjust the impact of certain Htrs or Htr clusters depending on its current needs or environmental conditions. Secondly, we propose a hypothetical feedback loop from the response regulator to Htr methylation made from the CheC proteins, CheD and CheB, which might contribute to adaptation analogous to the CheC/CheD system of B. subtilis.