Fluorescence recovery protein
From Wikipedia, the free encyclopedia
| Fluorescence recovery protein | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | FRP | ||||||
| Alt. symbols | slr1964 | ||||||
| PDB | 4JDX | ||||||
| UniProt | P74103 | ||||||
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Fluorescence recovery protein (FRP) is a small protein involved in regulating non-photochemical quenching in cyanobacteria. It prevents accumulation of the red photoactivated form of orange carotenoid protein (OCP), thereby reducing the amount of fluorescence quenching that occurs between the OCP and the phycobilisome antenna complexes.[1] It interacts with the C-terminal domain of OCP, which shares homology with the NTF2 superfamily.[2]
FRP is constitutively active, both in vivo and in vitro. It is able to prevent quenching of phycobilin fluorescence by OCP in vitro.[3] Overexpression of FRP in Synechocystis PCC 6803 leads to an absence of fluorescence quenching.[4] Deletion mutants of FRP show a slightly larger degree of fluorescence quenching induced by strong blue-green light, but was unable to restore fluorescence levels when transferred to low-light or darkness.[1]
Structure
The protein is all alpha-helical, and the protein structure from Synechocystis was solved in 2013, showing both a dimer as well as a tetramer form in the same crystal used for X-ray diffraction.[2] It is believed that the dimer is the active form. In the tetramer structure, one of the alpha helices is extended, disrupting the structure of a conserved patch of amino acids that is suggested to be an active site. Among these conserved residues, a histidine at position 53 and an arginine residue at position 60 have been shown to be essential for activity. Mutations in several other residues within this patch led to poor expression and precipitation, as well as loss of activity.