Blue news: NTP binding properties of the blue-light sensitive YtvA protein from Bacillus subtilis.
The blue-light sensitive protein YtvA from Bacillus subtilis is built of a photoactive, flavin-binding LOV (Light, Oxygen and Voltage) domain and a STAS domain with unknown function. Here we show that YtvA binds a fluorescent derivative of guanosine triphosphate (GTPTR) that can be displaced by both GTP or ATP. Unspecific NTP (N=G or A) binding is supported by the molecular model of YtvA-STAS. Blue-light activation of YtvA results in small and dark-reversible spectroscopic changes for GTPTR, suggesting that light-driven conformational changes are transmitted from the LOV core to the GTPTR binding site. These results support the idea that STAS domains may have a general NTP binding role and open a way to investigate the molecular functionality of YtvA-STAS.
Buttani
Valentina
V
Department of Physics, University of Parma, Italy.
Losi
Aba
A
Polverini
Eugenia
E
Gärtner
Wolfgang
W
D000255:Adenosine Triphosphate / Q000378:metabolism*; D001412:Bacillus subtilis / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000528:radiation effects; D003116:Color; D006160:Guanosine Triphosphate / Q000378:metabolism*; D008027:Light; D008958:Models, Molecular; D017433:Protein Structure, Secondary / Q000528:radiation effects; D017434:Protein Structure, Tertiary / Q000528:radiation effects; D017386:Sequence Homology, Amino Acid; D013050:Spectrometry, Fluorescence
D001426:Bacterial Proteins; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate