부산대학교 도서관

Abstract GFP-like proteins from lancelets (lanFPs) is a new and least studied group that already generated several outstanding biomarkers (mNeonGreen is the brightest FP to date) and has some unique features. Here, we report the study of four homologous lanFPs with GYG and GYA chromophores. Until recently, it was accepted that the third chromophore-forming residue in GFP-like proteins should be glycine, and efforts to replace it were in vain. Now, we have the first structure of a fluorescent protein with a successfully matured chromophore that has alanine as the third chromophore-forming residue. Consideration of the protein structures revealed two alternative routes of posttranslational transformation, resulting in either chromophore maturation or hydrolysis of GYG/GYA tripeptide. Both transformations are catalyzed by the same set of catalytic residues, Arg88 and Glu35–Wat–Glu211 cluster, whereas the residues in positions 62 and 102 shift the equilibrium between chromophore maturation and hydrolysis. Graphical Abstract Unlabelled Image Highlights • GFP-like fluorescent proteins from lancelet Branchiostoma floridae (lanFPs) have a mature chromophore with alanine as the third chromophore-forming residue (GYA). • In lanFPs, there are two alternative routes of posttranslational transformation, resulting in either chromophore maturation or hydrolysis of GYG/GYA tripeptide. • Both transformations are catalyzed by the same set of residues, Arg88 and Glu211–Wat–Glu35 cluster present in most lanFPs. • The residues in positions 62 and 102 rule the chromophore maturation/hydrolysis equilibrium. [ABSTRACT FROM AUTHOR]