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Function, structure and mechanism of bacterial photosensory LOV proteins

Journal

NATURE REVIEWS MICROBIOLOGY
Volume 9, Issue 10, Pages 713-723

Publisher

NATURE PORTFOLIO
DOI: 10.1038/nrmicro2622

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Funding

  1. US National Institutes of Health [1R01GM087353-3]
  2. Mallinckrodt Foundation
  3. Arnold and Mabel Beckman Foundation

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LOV (light, oxygen or voltage) domains are protein photosensors that are conserved in bacteria, archaea, plants and fungi, and detect blue light via a flavin cofactor. LOV domains are present in both chemotrophic and phototrophic bacterial species, in which they are found amino-terminally of signalling and regulatory domains such as sensor histidine kinases, diguanylate cyclases-phosphodiesterases, DNA-binding domains and regulators of RNA polymerase sigma-factors. In this Review, we describe the current state of knowledge about the function of bacterial LOV proteins, the structural basis of LOV domain-mediated signal transduction, and the use of LOV domains as genetically encoded photoswitches in synthetic biology.

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