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Nat Rev Microbiol. 2011 Aug 8;9(10):713-23. doi: 10.1038/nrmicro2622.

Function, structure and mechanism of bacterial photosensory LOV proteins.

Author information

1
Department of Biochemistry and Molecular Biology, The University of Chicago, Illinois 60637, USA.

Abstract

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 σ-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.

PMID:
21822294
PMCID:
PMC3286519
DOI:
10.1038/nrmicro2622
[Indexed for MEDLINE]
Free PMC Article

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