Abstract
Bacteriophytochromes (Bphs) are photoreceptors that help bacteria sense changes in light wavelength and intensity. Bphs contain a linear tetrapyrrole chromophore that, upon absorption of red or far-red light, undergoes a cis–trans isomerization that leads to a conformational change in the holoprotein. The conformation and type of Bph affects the expression of genes. The linear tetrapyrrole bound by Bphs is thought to come from O2-dependent cleavage of heme by a heme oxygenase. We have discovered that the absence of O2 does not inhibit the normal function of two Bphs in the regulation of Rhodopseudomonas palustris light-harvesting complexes. These observations imply that: (i) a linear tetrapyrrole can be made anaerobically, either through anaerobic heme cleavage by a novel enzyme or directly from the heme precursor hydroxymethylbilane without ring cleavage; or (ii) that Bph-dependent signal transduction does not require a chromophore.
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Acknowledgments
This research was supported by a Universitas 21 scholarship to ML and an NSERC Discovery grant to JTB. SN thanks Boehringer Ingelheim Fonds Travel Allowances for support. We thank L. Eltis for use of his anaerobic glovebox, and J. Johnson for expert technical assistance.
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Li, M., Noll, S. & Beatty, J.T. Bacteriophytochrome-Dependent Regulation of Light-Harvesting Complexes in Rhodopseudomonas palustris Anaerobic Cultures. Curr Microbiol 61, 429–434 (2010). https://doi.org/10.1007/s00284-010-9634-1
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DOI: https://doi.org/10.1007/s00284-010-9634-1