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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 and Gottfried Unden ORCID logo EMAIL logo
Published/Copyright: August 6, 2021
Biological Chemistry
From the journal Biological Chemistry Volume 402 Issue 10

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.

Keywords: DcuS; Escherichia coli ; oxidative Cys crosslinking; sensor kinase; transmembrane helix
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

© 2021 Walter de Gruyter GmbH, Berlin/Boston

Articles in the same Issue

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https://doi.org/10.1515/hsz-2021-0254
Keywords for this article
DcuS; Escherichia coli; oxidative Cys crosslinking; sensor kinase; transmembrane helix

Articles in the same Issue

  1. Frontmatter
  2. Review
  3. Biophysical applications in structural and molecular biology
  4. Research Articles/Short Communications
  5. Genes and Nucleic Acids
  6. Historic nucleic acids isolated by Friedrich Miescher contain RNA besides DNA
  7. Protein Structure and Function
  8. The extracellular region of bovine milk butyrophilin exhibits closer structural similarity to human myelin oligodendrocyte glycoprotein than to immunological BTN family receptors
  9. Structural insights into the repair mechanism of AGT for methyl-induced DNA damage
  10. Cell Biology and Signaling
  11. In vitro osteogenic activities of sulfated derivative of polysaccharide extracted from Tamarindus indica L.
  12. Synthesis and biological characterization of a new fluorescent probe for vesicular trafficking based on polyazamacrocycle derivative
  13. Properties of transmembrane helix TM1 of the DcuS sensor kinase of Escherichia coli, the stator for TM2 piston signaling
  14. Lefty A is involved in sunitinib resistance of renal cell carcinoma cells via regulation of IL-8
  15. Proteolysis
  16. Tissue factor pathway inhibitor 2 is a potent kallikrein-related protease 12 inhibitor
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