Major colour patterns of reef-building corals are due to a family of GFP-like proteins |
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Authors: | S G Dove O Hoegh-Guldberg S Ranganathan |
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Institution: | (1) Centre for Marine Studies, University of Queensland, 4072 QLD, Australia e-mail: sophie@mailbox.uq.edu.au, AU;(2) Australian Genomic Information Centre, University of Sydney, 2006 NSW, Australia, AU |
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Abstract: | Reef-building corals are renowned for their brilliant colours yet the biochemical basis for the pigmentation of corals is
unknown. Here, we show that these colours are due to a family of GFP-like proteins that fluoresce under ultraviolet (UV) or
visible light. Pigments from ten coral species were almost identical to pocilloporin (Dove et al. 1995) being dimers or trimers
with approximately 28-kDa subunits. Degenerative primers made to common N-terminal sequences yielded a complete sequence from
reef-building coral cDNA, which had 19.6% amino acid identity with green fluorescent protein (GFP). Molecular modelling revealed
a `β-can' structure, like GFP, with 11 β-strands and a completely solvent-inaccessible fluorophore composed of the modified
residues Gln-61, Tyr-62 and Gly-63. The molecular properties of pocilloporins indicate a range of functions from the conversion
of high-intensity UV radiation into photosynthetically active radiation (PAR) that can be regulated by the dinoflagellate
peridinin-chlorophyll-protein (PCP) complex, to the shielding of the Soret and Qx bands of chlorophyll a and c from scattered high-intensity light. These properties of pocilloporin support its potential role in protecting the photosynthetic
machinery of the symbiotic dinoflagellates of corals under high light conditions and in enhancing the availability of photosynthetic
light under shade conditions.
Accepted: 29 May 2000 |
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Keywords: | Reef-building coral Pigments GFP Photoprotection Photosynthetic accessory pigments |
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