Structural highlights
Function
RFP_DISSP Thought to play a role in photoprotection of the coral's resident symbiont microalgae's photosystems from photoinhibition caused by high light levels found near the surface of coral reefs. In deeper water, the fluorescence may be to convert blue light into longer wavelengths more suitable for use in photosynthesis by the microalgal symbionts.[1]
Publication Abstract from PubMed
We report the evolution of mScarlet3, a cysteine-free monomeric red fluorescent protein with fast and complete maturation, as well as record brightness, quantum yield (75%) and fluorescence lifetime (4.0 ns). The mScarlet3 crystal structure reveals a barrel rigidified at one of its heads by a large hydrophobic patch of internal residues. mScarlet3 behaves well as a fusion tag, displays no apparent cytotoxicity and it surpasses existing red fluorescent proteins as a Forster resonance energy transfer acceptor and as a reporter in transient expression systems.
mScarlet3: a brilliant and fast-maturing red fluorescent protein.,Gadella TWJ Jr, van Weeren L, Stouthamer J, Hink MA, Wolters AHG, Giepmans BNG, Aumonier S, Dupuy J, Royant A Nat Methods. 2023 Mar 27. doi: 10.1038/s41592-023-01809-y. PMID:36973546[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matz MV, Fradkov AF, Labas YA, Savitsky AP, Zaraisky AG, Markelov ML, Lukyanov SA. Fluorescent proteins from nonbioluminescent Anthozoa species. Nat Biotechnol. 1999 Oct;17(10):969-73. PMID:10504696 doi:http://dx.doi.org/10.1038/13657
- ↑ Gadella TWJ Jr, van Weeren L, Stouthamer J, Hink MA, Wolters AHG, Giepmans BNG, Aumonier S, Dupuy J, Royant A. mScarlet3: a brilliant and fast-maturing red fluorescent protein. Nat Methods. 2023 Apr;20(4):541-545. PMID:36973546 doi:10.1038/s41592-023-01809-y
