A family of GFP-like proteins with different spectral properties in lancelet <Emphasis Type="Italic">Branchiostoma floridae</Emphasis> |
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| Authors: | Diana Baumann Malcolm Cook Limei Ma Arcady Mushegian Erik Sanders Joel Schwartz C Ron Yu |
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| Institution: | (1) Stowers Institute for Medical Research, 1000 E 50th St., Kansas City, MO 64110, USA;(2) Department of Microbiology, Molecular Genetics, and Immunology, University of Kansas, Kansas City, KS 66160, USA;(3) Department of Anatomy and Cell Biology, University of Kansas Medical Center, Kansas City, KS 66160, USA |
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| Abstract: | Background Members of the green fluorescent protein (GFP) family share sequence similarity and the 11-stranded β-barrel fold. Fluorescence
or bright coloration, observed in many members of this family, is enabled by the intrinsic properties of the polypeptide chain
itself, without the requirement for cofactors. Amino acid sequence of fluorescent proteins can be altered by genetic engineering
to produce variants with different spectral properties, suitable for direct visualization of molecular and cellular processes.
Naturally occurring GFP-like proteins include fluorescent proteins from cnidarians of the Hydrozoa and Anthozoa classes, and from copepods of the Pontellidae family, as well as non-fluorescent proteins from Anthozoa. Recently, an mRNA encoding a fluorescent GFP-like protein AmphiGFP, related to GFP from Pontellidae, has been isolated from the lancelet Branchiostoma floridae, a cephalochordate (Deheyn et al., Biol Bull, 2007 213:95). |
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