Function, structure and mechanism of bacterial photosensory LOV proteins

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

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.

Publication types

  • Review

MeSH terms

  • Archaea / chemistry
  • Archaea / genetics
  • Archaea / metabolism
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / metabolism
  • Bacteria* / chemistry
  • Bacteria* / genetics
  • Bacteria* / metabolism
  • Bacterial Proteins* / chemistry
  • Bacterial Proteins* / metabolism
  • Cryptochromes
  • Flavins / metabolism
  • Flavoproteins / chemistry
  • Flavoproteins / metabolism
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism
  • Fungi / chemistry
  • Fungi / genetics
  • Fungi / metabolism
  • Light
  • Phototropins / metabolism
  • Phototropism*
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism
  • Plants / chemistry
  • Plants / genetics
  • Plants / metabolism
  • Signal Transduction
  • Synthetic Biology

Substances

  • Archaeal Proteins
  • Bacterial Proteins
  • Cryptochromes
  • Flavins
  • Flavoproteins
  • Fungal Proteins
  • Phototropins
  • Plant Proteins