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Fluorescent proteins have become essential tools in molecular and biologi-cal applications. Here, we present a novel fluorescent protein isolated from warm water coral, Cyphastrea microphthalma. The protein, which we named vivid Verde fluorescent protein (VFP), matures readily at 37 C and emits bright green light. | ỊFEBS Journal A new bright green-emitting fluorescent protein -engineered monomeric and dimeric forms Robielyn P. Ilagan1 Elizabeth Rhoades1 David F. Gruber2 Hung-Teh Kao3 Vincent A. Pieribone4 and Lynne Regan1 5 1 Department of Molecular Biophysics and Biochemistry Yale University New Haven CT USA 2 Department of NaturalSciences Baruch College and The Graduate Center City University of New York NY USA 3 Department of Psychiatry and Human Behavior Brown University Providence RI USA 4 The John B. Pierce Laboratory Yale University New Haven CT USA 5 Department of Chemistry Yale University New Haven CT USA Keywords detection marker fluorescence correlation spectroscopy fluorescent protein oligomeric states relative brightness Correspondence L. Regan Department of Molecular Biophysics and Biochemistry Yale University New Haven CT 06520 USA Fax 203 432 5175 Tel 203 432 9843 E-mail lynne.regan@yale.edu Note The nucleotide sequence data are available in the DDBJ EMBL GenBank databases under the accession number FN597286 and the protein sequence data are in Uni-ProtKB TrEMBL with the accession number D1J6P8. Received 22 December 2009 revised 5 February 2010 accepted 15 February 2010 doi 10.1111 j.1742-4658.2010.07618.x Fluorescent proteins have become essential tools in molecular and biological applications. Here we present a novel fluorescent protein isolated from warm water coral Cyphastrea microphthalma. The protein which we named vivid Verde fluorescent protein VFP matures readily at 37 C and emits bright green light. Further characterizations revealed that VFP has a tendency to form dimers. By creating a homology model of VFP based on the structure of the red fluorescent protein DsRed we were able to make mutations that alter the protein s oligomerization state. We present two proteins mVFP and mVFP1 that are both exclusively monomeric and one protein dVFP which is dimeric. We characterized the spectroscopic properties of VFP and its variants in comparison with .
