Dynamic Regulation of Fluorescent Proteins from a Single Species of Coral

• Published in: Marine biotechnology (New York, N.Y.) Vol. 9; no. 6; pp. 733 - 746
• Main Authors: Kao, Hung-Teh, Sturgis, Shelby, DeSalle, Rob, Tsai, Julia, Davis, Douglas, Gruber, David F, Pieribone, Vincent A
• Format: Journal Article
• Language: English
• Published: United States New York : Springer-Verlag 01.12.2007; Springer Nature B.V
• Subjects: Animals; Anthozoa - chemistry; Anthozoa - genetics; Anthozoa - physiology; Atolls; barrier reef; Base Sequence; coordinate expression; depth; DNA Primers - chemistry; Environment; Gene Expression Profiling - veterinary; Gene Expression Regulation - physiology; Luminescent Proteins - biosynthesis; Luminescent Proteins - genetics; Luminescent Proteins - physiology; Molecular Sequence Data; Montastraea cavernosa; Phylogeny; Pigmentation; Proteins; real-time quantitative PCR; Reproducibility of Results; Reverse Transcriptase Polymerase Chain Reaction - veterinary; RNA, Ribosomal, 18S - analysis; Sensitivity and Specificity; Statistics as Topic; Tubulin - analysis; Tubulin - biosynthesis; Belize
• ISSN: 1436-2228; 1436-2236
• DOI: 10.1007/s10126-007-9025-1

To gain a better understanding of the natural function of fluorescent proteins, we have undertaken quantitative analyses of these proteins in a single species of coral, Montastraea cavernosa, residing around Turneffe atoll, on the Belizean Barrier Reef. We identified at least 10 members of a fluorescent protein family in this species, which consist of 4 distinct spectral classes. As much as a 10-fold change in the overall expression of fluorescent proteins was observed from specimen to specimen, suggesting that fluorescent proteins are dynamically regulated in response to environmental or physiological conditions. We found that the expression of some proteins was inversely correlated with depth, and that groups of proteins were coordinately expressed. There was no relationship between the expression of fluorescent proteins and the natural coloration of the Montastraea cavernosa specimens in this study. These findings have implications for current hypotheses regarding the properties and natural function of fluorescent proteins.