Universität zu Köln

Glantz, Spencer T., Carpenter, Eric J., Melkonian, Michael, Gardner, Kevin H. ORCID: 0000-0002-8671-2556, Boyden, Edward S., Wong, Gane Ka-Shu and Chow, Brian Y. (2016). Functional and topological diversity of LOV domain photoreceptors. Proc. Natl. Acad. Sci. U. S. A., 113 (11). S. E1442 - 10. WASHINGTON: NATL ACAD SCIENCES. ISSN 0027-8424

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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 similar to 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 a-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.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Glantz, Spencer T. UNSPECIFIED UNSPECIFIED UNSPECIFIED Carpenter, Eric J. UNSPECIFIED UNSPECIFIED UNSPECIFIED Melkonian, Michael UNSPECIFIED UNSPECIFIED UNSPECIFIED Gardner, Kevin H. UNSPECIFIED orcid.org/0000-0002-8671-2556 UNSPECIFIED Boyden, Edward S. UNSPECIFIED UNSPECIFIED UNSPECIFIED Wong, Gane Ka-Shu UNSPECIFIED UNSPECIFIED UNSPECIFIED Chow, Brian Y. UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-281389
DOI:	10.1073/pnas.1509428113
Journal or Publication Title:	Proc. Natl. Acad. Sci. U. S. A.
Volume:	113
Number:	11
Page Range:	S. E1442 - 10
Date:	2016
Publisher:	NATL ACAD SCIENCES
Place of Publication:	WASHINGTON
ISSN:	0027-8424
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language SENSOR HISTIDINE KINASE; PHOTOACTIVE YELLOW PROTEIN; BLUE-LIGHT PHOTORECEPTOR; FULL-LENGTH STRUCTURE; WHITE-COLLAR COMPLEX; SIGNALING MECHANISM; STRUCTURAL BASIS; CONFORMATIONAL-CHANGES; TRANSCRIPTION FACTOR; GENE-EXPRESSION Multiple languages Multidisciplinary Sciences Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/28138