Functional and topological diversity of LOV domain photoreceptors

Spencer T. Glantz, Eric J. Carpenter, Michael Melkonian, Kevin H. Gardner, Edward S. Boyden, Gane Ka Shu Wong, Brian Y. Chow

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Light-oxygen-voltage sensitive (LOV) flavoproteins are ubiquitous photoreceptors that mediate responses to environmental cues. Photosensory inputs are transduced into signaling outputs via structural rearrangements in sensor domains that consequently modulate the activity of an effector domain or multidomain clusters. Establishing the diversity in effector function and sensor-effector topology will inform what signaling mechanisms govern light-responsive behaviors across multiple kingdoms of life and how these signals are transduced. Here, we report the bioinformatics identification of over 6,700 candidate LOV domains (including over 4,000 previously unidentified sequences from plants and protists), and insights from their annotations for ontological function and structural arrangements. Motif analysis identified the sensors from ∼42 million ORFs, with strong statistical separation from other flavoproteins and non-LOV members of the structurally related Per-aryl hydrocarbon receptor nuclear translocator (ARNT)-Sim family. Conserved-domain analysis determined putative light-regulated function and multidomain topologies. We found that for certain effectors, sensor-effector linker length is discretized based on both phylogeny and the preservation of α-helical heptad repeats within an extended coiled-coil linker structure. This finding suggests that preserving sensor-effector orientation is a key determinant of linker length, in addition to ancestry, in LOV signaling structure-function.We found a surprisingly high prevalence of effectors with functions previously thought to be rare among LOV proteins, such as regulators of G protein signaling, and discovered several previously unidentified effectors, such as lipases. This work highlights the value of applying genomic and transcriptomic technologies to diverse organisms to capture the structural and functional variation in photosensory proteins that are vastly important in adaptation, photobiology, and optogenetics.

Original languageEnglish (US)
Pages (from-to)E1442-E1451
JournalProceedings of the National Academy of Sciences of the United States of America
Volume113
Issue number11
DOIs
StatePublished - Mar 15 2016

Fingerprint

Oxygen
Light
Flavoproteins
Aryl Hydrocarbon Receptor Nuclear Translocator
Photobiology
Optogenetics
GTP-Binding Protein Regulators
Phylogeny
Computational Biology
Lipase
Open Reading Frames
Cues
Proteins
Technology

Keywords

  • Flavoproteins
  • LOV
  • Optogenetics
  • Photoreceptors

ASJC Scopus subject areas

  • General

Cite this

Functional and topological diversity of LOV domain photoreceptors. / Glantz, Spencer T.; Carpenter, Eric J.; Melkonian, Michael; Gardner, Kevin H.; Boyden, Edward S.; Wong, Gane Ka Shu; Chow, Brian Y.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 113, No. 11, 15.03.2016, p. E1442-E1451.

Research output: Contribution to journalArticle

Glantz, Spencer T. ; Carpenter, Eric J. ; Melkonian, Michael ; Gardner, Kevin H. ; Boyden, Edward S. ; Wong, Gane Ka Shu ; Chow, Brian Y. / Functional and topological diversity of LOV domain photoreceptors. In: Proceedings of the National Academy of Sciences of the United States of America. 2016 ; Vol. 113, No. 11. pp. E1442-E1451.
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