Chromophore composition of a heterologously expressed BLUF-domain.
Upon heterologous expression of the BLUF (for: Blue-Light sensing Using Flavin) domain from AppA, a transcriptional anti-repressor from Rhodobacter sphaeroides, in Escherichia coli, photoactive holo-protein is formed through non-covalent binding of a flavin. Whereas it is generally assumed that FAD is the physiological chromophore of this photo-perception domain in vivo, E. coli can (and does) insert, depending on the growth conditions, all naturally occurring flavins, i.e. riboflavin, FMN and FAD into this protein domain. The nature of the particular flavin bound affects the photochemical- and particularly the fluorescence properties of the N-terminal domain of this photosensory protein.
Laan
Wouter
W
Laboratory for Microbiology, Swammerdam Institute for Life Sciences, Nieuwe Achtergracht 166, NL-1018 WV, Amsterdam, The Netherlands. Laan@science.uva.nl
Bednarz
Teresa
T
Heberle
Joachim
J
Hellingwerf
Klaas J
KJ
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000528:radiation effects; D003001:Cloning, Molecular; D004926:Escherichia coli; D005420:Flavoproteins / Q000737:chemistry / Q000235:genetics* / Q000528:radiation effects; D008027:Light; D011994:Recombinant Proteins / Q000737:chemistry / Q000528:radiation effects; D012242:Rhodobacter sphaeroides; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared
C116785:AppA protein, Rhodobacter sphaeroides; D001426:Bacterial Proteins; D005420:Flavoproteins; D011994:Recombinant Proteins