Research article

Amphioxus encodes the largest known family of green fluorescent proteins, which have diversified into distinct functional classes

Erin K Bomati¹ , Gerard Manning² and Dimitri D Deheyn¹

¹  Scripps Institution of Oceanography, University of California San Diego, La Jolla, CA 92093, USA

²  Razavi Newman Center for Bioinformatics, Salk Institute for Biological Studies, La Jolla, CA 92037, USA

author email corresponding author email

BMC Evolutionary Biology 2009, 9:77doi:10.1186/1471-2148-9-77

Published:	21 April 2009

Abstract

Background

Green fluorescent protein (GFP) has been found in a wide range of Cnidaria, a basal group of metazoans in which it is associated with pigmentation, fluorescence, and light absorbance. A GFP has been recently discovered in the pigmentless chordate Branchiostoma floridae (amphioxus) that shows intense fluorescence mainly in the head region.

Results

The amphioxus genome encodes 16 closely-related GFP-like proteins, all of which appear to be under purifying selection. We divide them into 6 clades based on protein sequence identity and show that representatives of each clade have significant differences in fluorescence intensity, extinction coefficients, and absorption profiles. Furthermore, GFPs from two clades exhibit antioxidant capacity. We therefore propose that amphioxus GFPs have diversified their functions into fluorescence, redox, and perhaps just light absorption in relation to pigmentation and/or photoprotection.

Conclusion

The rapid radiation of amphioxus GFP into clades with distinct functions and spectral properties reveals functional plasticity of the GFP core. The high sequence similarities between different clades provide a model system to map sequence variation to functional changes, to better understand and engineer GFP.