Abstract.
We have recently discovered heme-containing signal transducers from the archaeon Halobacterium salinarum (HemAT-Hs) and the gram-positive bacterium Bacillus subtilis (HemAT-Bs). These proteins bind diatomic oxygen and trigger aerotactic responses. We identified that HemAT oxygen-sensing domains contain a globin-coupled sensor (GCS) motif, which exists as a two-domain transducer, having no similarity to the PAS domain (Period circadian protein, Ah receptor nuclear translocator protein, Single-minded protein) superfamily transducers. Using the GCS motif, we predicted that a 439-amino-acid protein annotated as a methyl-accepting chemotaxis protein (MCP) in the facultatively alkaliphilic bacterium Bacillus halodurans is a globin-coupled oxygen sensor. We cloned, expressed, and purified GCS Bh and performed its spectral analysis. GCS Bh binds heme and shows myoglobin-like spectra. This suggests that GCS Bh acts as an oxygen sensor and transmits a conformational signal through a linked signaling domain to trigger an aerotactic response in B. halodurans.
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Hou, S., Belisle, C., Lam, S. et al. A globin-coupled oxygen sensor from the facultatively alkaliphilic Bacillus halodurans C-125. Extremophiles 5, 351–354 (2001). https://doi.org/10.1007/s007920100220
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DOI: https://doi.org/10.1007/s007920100220