Mechanisms of protein fluorophore formation and engineering.
Green fluorescent protein (GFP) from the jellyfish Aequorea victoria and GFP-like proteins from Anthozoa species contain light-absorbing chromophores within their protein sequences. Recent studies have made progress in obtaining bright variants of these proteins that develop chromophores quickly and efficiently, as well as novel fluorescent proteins that photoconvert (i.e. change color upon illumination at specific wavelengths). Further molecular characterization of the structure and maturation of these proteins is in progress, aimed at providing information for rational design of variants with desired fluorescence properties.
Laboratory for Cell Function Dynamics, Advanced Technology Development Group, Brain Science Institute, RIKEN, 2-1 Hirosawa, Wako-city, Saitama 351-0198, Japan. matsushi@brain.riken.go.jp
Atsushi
A
Miyawaki
Takeharu
T
Nagai
Hideaki
H
Mizuno
D000818:Animals; D001426:Bacterial Proteins / Q000138:chemical synthesis / Q000235:genetics / Q000378:metabolism; D005456:Fluorescent Dyes / Q000737:chemistry; D049452:Green Fluorescent Proteins; D008164:Luminescent Proteins / Q000138:chemical synthesis* / Q000235:genetics / Q000378:metabolism*; D015394:Molecular Structure; D015202:Protein Engineering / Q000379:methods*
D001426:Bacterial Proteins; D005456:Fluorescent Dyes; D008164:Luminescent Proteins; C413663:fluorescent protein 583; C054562:yellow fluorescent protein, Bacteria; D049452:Green Fluorescent Proteins