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Structural features discriminating hybrid histidine kinase Rec domains from response regulator homologs

Author

Listed:
  • Mitchell Brüderlin

    (University of Basel)

  • Raphael Böhm

    (University of Basel)

  • Firas Fadel

    (University of Basel)

  • Sebastian Hiller

    (University of Basel)

  • Tilman Schirmer

    (University of Basel)

  • Badri N. Dubey

    (University of Basel
    CSSB Centre for Structural Systems Biology, Deutsches Elektronen-Synchrotron DESY)

Abstract

In two-component systems, the information gathered by histidine kinases (HKs) are relayed to cognate response regulators (RRs). Thereby, the phosphoryl group of the auto-phosphorylated HK is transferred to the receiver (Rec) domain of the RR to allosterically activate its effector domain. In contrast, multi-step phosphorelays comprise at least one additional Rec (Recinter) domain that is typically part of the HK and acts as an intermediary for phosphoryl-shuttling. While RR Rec domains have been studied extensively, little is known about discriminating features of Recinter domains. Here we study the Recinter domain of the hybrid HK CckA by X-ray crystallography and NMR spectroscopy. Strikingly, all active site residues of the canonical Rec-fold are pre-arranged for phosphoryl-binding and BeF3- binding does not alter secondary or quaternary structure, indicating the absence of allosteric changes, the hallmark of RRs. Based on sequence-covariation and modeling, we analyze the intra-molecular DHp/Rec association in hybrid HKs.

Suggested Citation

  • Mitchell Brüderlin & Raphael Böhm & Firas Fadel & Sebastian Hiller & Tilman Schirmer & Badri N. Dubey, 2023. "Structural features discriminating hybrid histidine kinase Rec domains from response regulator homologs," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36597-8
    DOI: 10.1038/s41467-023-36597-8
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    References listed on IDEAS

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    1. Emanuele G. Biondi & Sarah J. Reisinger & Jeffrey M. Skerker & Muhammad Arif & Barrett S. Perchuk & Kathleen R. Ryan & Michael T. Laub, 2006. "Regulation of the bacterial cell cycle by an integrated genetic circuit," Nature, Nature, vol. 444(7121), pages 899-904, December.
    2. Raphael D. Teixeira & Fabian Holzschuh & Tilman Schirmer, 2021. "Activation mechanism of a small prototypic Rec-GGDEF diguanylate cyclase," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    3. C. Lori & S. Ozaki & S. Steiner & R. Böhm & S. Abel & B. N. Dubey & T. Schirmer & S. Hiller & U. Jenal, 2015. "Cyclic di-GMP acts as a cell cycle oscillator to drive chromosome replication," Nature, Nature, vol. 523(7559), pages 236-239, July.
    4. F. Pontiggia & D.V. Pachov & M.W. Clarkson & J. Villali & M.F. Hagan & V.S. Pande & D. Kern, 2015. "Free energy landscape of activation in a signalling protein at atomic resolution," Nature Communications, Nature, vol. 6(1), pages 1-14, November.
    5. Andreas Kaczmarczyk & Antje M. Hempel & Christoph Arx & Raphael Böhm & Badri N. Dubey & Jutta Nesper & Tilman Schirmer & Sebastian Hiller & Urs Jenal, 2020. "Precise timing of transcription by c-di-GMP coordinates cell cycle and morphogenesis in Caulobacter," Nature Communications, Nature, vol. 11(1), pages 1-16, December.
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