Evidence for multiple phototransduction pathways in a reef-building coral

Autor: Vladlen Z. Slepak, Michael C. Schmale, Margaret W. Miller, Valery I. Shestopalov, Benjamin Mason, Qiang Wang, Konstantin Levay, Patrick D.L. Gibbs
Jazyk: angličtina
Rok vydání: 2012
Předmět:
0106 biological sciences
Opsin
Coral
Marine and Aquatic Sciences
lcsh:Medicine
Ectoderm
01 natural sciences
Biochemistry
Molecular Cell Biology
Trypsin
Cloning
Molecular
lcsh:Science
0303 health sciences
Multidisciplinary
biology
Ecology
Coral Reefs
Marine Ecology
Anthozoa
Cell biology
medicine.anatomical_structure
Corals
Endoderm
Visual phototransduction
Research Article
Light Signal Transduction
G protein
Animal Types
Molecular Sequence Data
Marine Biology
010603 evolutionary biology
03 medical and health sciences
medicine
Acropora
Animals
Humans
14. Life underwater
Amino Acid Sequence
Biology
030304 developmental biology
Evolutionary Biology
Opsins
Sequence Homology
Amino Acid
fungi
lcsh:R
Proteins
Aquatic Environments
biology.organism_classification
Elkhorn coral
Transmembrane Proteins
Microscopy
Fluorescence
Proteolysis
Earth Sciences
Veterinary Science
lcsh:Q
Ecological Environments
Aquatic Animals
Zdroj: PLoS ONE, Vol 7, Iss 12, p e50371 (2012)
PLoS ONE
ISSN: 1932-6203
Popis: Photosensitive behaviors and circadian rhythms are well documented in reef-building corals and their larvae, but the mechanisms responsible for photoreception have not been described in these organisms. Here we report the cloning, immunolocalization, and partial biochemical characterization of three opsins and four G proteins expressed in planulae of the Caribbean elkhorn coral, Acropora palmata. All three opsins (acropsins 1-3) possess conserved seven-pass transmembrane structure, and localize to distinct regions of coral planulae. Acropsin 1 was localized in the larval endoderm, while acropsin 2 was localized in solitary cells of the ectoderm. These rod-like cells displayed a remarkably polarized distribution, concentrated in the aboral end. We also cloned four A. palmata G protein alpha subunits. Three were homologs of vertebrate Gi, Go, and Gq. The fourth is presumably a novel G protein, which displays only 40% identity with the nearest known G protein, and we termed it Gc for "cnidarian". We show that Gc and Gq can be activated by acropsins in a light-dependent manner in vitro. This indicates that at least acropsins 1 and 3 can form functional photoreceptors and potentially may play a role in color preference during settlement, vertical positioning and other light-guided behaviors observed in coral larvae.
Databáze: OpenAIRE
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