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<p>The nutrient germinant receptors (GRs) in spores of <i>Bacillus</i> species consist of a cluster of three proteins– designated A, B, and C subunits– that play a critical role in initiating the germination of dormant spores in response to specific nutrient molecules. The <i>Bacillus cereus</i> GerI GR is essential for inosine-induced germination; however, the roles of the individual subunits and the mechanism by which germinant binding activates GR function remain unclear. In this study, we report the backbone chemical shift assignments of the N-terminal domain (NTD) of the A subunit of GerI (GerIA<sup>NTD</sup>). Furthermore, we derive the secondary structure of GerIA<sup>NTD</sup> in solution and compare it with the crystal structure of the NTD of the A subunit of a <i>Bacillus megaterium</i> GR. These findings lay the foundation for further NMR studies aimed at investigating the structure-function relationship of the GerI subunits, with a broader goal of understanding the molecular mechanism underlying germinant recognition and signal transduction in GRs across <i>Bacillus</i> species.</p>

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Backbone assignment of the N-terminal domain of the A subunit of the Bacillus cereus GerI germinant receptor

  • 期刊论文

  • 发表日期：

    2025年1月18日

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  • Yulia Pustovalova,
  • Yunfeng Li,
  • Jeffrey C. Hoch,
  • Bing Hao

摘要

The nutrient germinant receptors (GRs) in spores of Bacillus species consist of a cluster of three proteins– designated A, B, and C subunits– that play a critical role in initiating the germination of dormant spores in response to specific nutrient molecules. The Bacillus cereus GerI GR is essential for inosine-induced germination; however, the roles of the individual subunits and the mechanism by which germinant binding activates GR function remain unclear. In this study, we report the backbone chemical shift assignments of the N-terminal domain (NTD) of the A subunit of GerI (GerIANTD). Furthermore, we derive the secondary structure of GerIANTD in solution and compare it with the crystal structure of the NTD of the A subunit of a Bacillus megaterium GR. These findings lay the foundation for further NMR studies aimed at investigating the structure-function relationship of the GerI subunits, with a broader goal of understanding the molecular mechanism underlying germinant recognition and signal transduction in GRs across Bacillus species.