Startseite Properties of transmembrane helix TM1 of the DcuS sensor kinase of Escherichia coli, the stator for TM2 piston signaling
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Properties of transmembrane helix TM1 of the DcuS sensor kinase of Escherichia coli, the stator for TM2 piston signaling

  • Marius Stopp ORCID logo , Philipp A. Steinmetz und Gottfried Unden ORCID logo EMAIL logo
Veröffentlicht/Copyright: 6. August 2021

Abstract

The sensor kinase DcuS of Escherichia coli perceives extracellular fumarate by a periplasmic PASP sensor domain. Transmembrane (TM) helix TM2, present as TM2-TM2′ homo-dimer, transmits fumarate activation in a piston-slide across the membrane. The second TM helix of DcuS, TM1, is known to lack piston movement. Structural and functional properties of TM1 were analyzed. Oxidative Cys-crosslinking (CL) revealed homo-dimerization of TM1 over the complete membrane, but only the central part showed α-helical +3/+4 spacing of the CL maxima. The GALLEX bacterial two-hybrid system indicates TM1/TM1′ interaction, and the presence of a TM1-TM1′ homo-dimer is suggested. The peripheral TM1 regions presented CL in a spacing atypical for α-helical arrangement. On the periplasmic side the deviation extended over 11 AA residues (V32-S42) between the α-helical part of TM1 and the onset of PASP. In the V32-S42 region, CL efficiency decreased in the presence of fumarate. Therefore, TM1 exists as a homo-dimer with α-helical arrangement in the central membrane region, and non-α-helical arrangement in the connector to PASP. The fumarate induced structural response in the V32-S42 region is suggested to represent a structural adaptation to the shift of TM2 in the TM1-TM1′/TM2-TM2′ four-helical bundle.


Corresponding author: Gottfried Unden, Microbiology and Wine Research, Institute for Molecular Physiology, Johannes Gutenberg University Mainz, BZ II, Hanns-Dieter-Hüsch-Weg 17, D-55128 Mainz, Germany, E-mail:

Funding source: Deutsche Forschungsgemeinschaft 10.13039/501100001659

Award Identifier / Grant number: UN 49/21-1

Acknowledgments

We are grateful to Dr. D. Steindorf (Mainz) for help with experiments, and Dr. D. Schneider (Mainz) for helpful discussions.

  1. Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: Financial support was received by a grant of Deutsche Forschungsgemeinschaft (UN 49/21-1).

  3. Conflict of interest statement: The authors declare no conflicts of interest regarding this article.

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Supplementary Material

The online version of this article offers supplementary material (https://doi.org/10.1515/hsz-2021-0254).


Received: 2021-05-07
Accepted: 2021-07-05
Published Online: 2021-08-06
Published in Print: 2021-09-27

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