Meeting Abstract
GFP was one of the most useful discoveries of the 20th Century, due to its subsequent use in cell and molecular tagging applications, resulting in three Nobel Prizes in 2008 (Noble Media AB 2014). GFP and similar proteins, including anthozoan fluorescent proteins, have been used in numerous research efforts to probe cellular structure and function since its introduction. We have discovered a similar protein in a variant of the common anemone, Calliactis tricolor, from the Alabama Gulf Coast, which, unlike other anthozoan fluorescent proteins (Curr. Opin. Chem. Biol. 20:92; Curr. Opin. Biol. 12:505), is extraordinarily long-lived and resilient. The anemone’s mouth and mesenteries produce intense orange fluorescence, peak emission at 510 nm and 570 nm when illuminated by blue light at 500 nm and 540 nm. The protein appears to be freely associated with the cytoplasmic space of mesentery cells; purification of the protein yields a ~10S trimeric quaternary complex with three bands at 31, 25 and 10 kDa as revealed by SDS-PAGE. LC-MS/MS reveals that the fluorescence moiety is novel and has effectively no homology to any previously known fluorescent protein; moreover the fluorescent group is found only in the largest subunit. Ongoing whole genome analysis and differential transcriptomic analyses seek to reveal genome organization and appropriate regulatory elements and should provide data for future incorporation of this group into cellular probes. Our work reveals that this is a very easy to purify, resilient and easily handled protein and a look into genome organization and identification. Funds: Internal Grants Program, OVPR, Auburn Univ.
