Yellow fluorescent protein
Yellow fluorescent protein (YFP) is a genetic mutant of green fluorescent protein (GFP) originally derived from the jellyfish Aequorea victoria.[1] Its excitation peak is 513 nm and its emission peak is 527 nm.[2] Like the parent GFP, YFP is a useful tool in cell and molecular biology because the excitation and emission peaks of YFP are distinguishable from GFP which allows for the study of multiple processes/proteins within the same experiment.
Three improved versions of YFP are Citrine, Venus, and Ypet. They have reduced chloride sensitivity, faster maturation, and increased brightness (defined as the product of the
"Venus" contains a novel amino acid substitution –F46L– which accelerates the oxidation of the chromophore at 37°C, the rate limiting step of maturation. The protein has other substitutions (F64L/ M153T/ V163A/ S175G), permitting Venus to fold well and giving it relative tolerance to acidosis and Cl−.[3]
Evolution of YFP from GFP
Four protein mutations from the wild-type GFP found in Aequorea Victoria jellyfish were needed to create the YFP mutant. The most important mutation was the replacement of threonine with tyrosine at residue position 203[1] (the substitution is denoted by T203Y, where T and Y represent the single letter code for the amino acids threonine and tyrosine, respectively).
See also
References
- ^ PMID 8703075.
- ^ Lambert, Talley. "EYFP at FPbase". FPbase. Retrieved 2021-02-22.
- PMID 11753368.
External links
- Introduction to fluorescent proteins
- EYFP on FPbase
- Miyawaki, Atsushi; Llopis, Juan; Heim, Roger; McCaffery, J. Michael; Adams, Joseph A.; Ikura, Mitsuhiko; Tsien, Roger Y. (1997). "Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin". Nature. 388 (6645): 882–7. PMID 9278050.