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

Schlesner, M., Miller, A., Besir, H., Aivaliotis, M., Streif, J., Scheffer, B., et al. (2012). The protein interaction network of a taxis signal transduction system in a Halophilic Archaeon. BMC MICROBIOLOGY, 12: 272. doi:10.1186/1471-2180-12-272.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-ED62-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-ED63-8
Genre: Journal Article

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 Creators:
Schlesner, Matthias1, Author              
Miller, Arthur1, Author              
Besir, Hüseyin1, Author              
Aivaliotis, Michalis1, Author              
Streif, Judith1, Author              
Scheffer, Beatrix1, Author              
Siedler, Frank1, 2, Author              
Oesterhelt, Dieter1, Author              
Affiliations:
1Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565164              
2Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              

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Free keywords: ACCEPTING CHEMOTAXIS PROTEINS; SENSORY RHODOPSIN-I; BACILLUS-SUBTILIS CHEMOTAXIS; ESCHERICHIA-COLI CHEMOTAXIS; TANDEM MASS-SPECTROMETRY; SALINARUM STRAIN R1; HALOBACTERIUM-SALINARUM; BACTERIAL CHEMOTAXIS; HALOFERAX-VOLCANII; FLAGELLAR SWITCH
 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.

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Language(s): eng - English
 Dates: 2012-11-21
 Publication Status: Published online
 Pages: 20
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000315463100001
DOI: 10.1186/1471-2180-12-272
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Title: BMC MICROBIOLOGY
Source Genre: Journal
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Publ. Info: 236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLAND : BIOMED CENTRAL LTD
Pages: - Volume / Issue: 12 Sequence Number: 272 Start / End Page: - Identifier: ISSN: 1471-2180