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Blue news: NTP binding properties of the blue‐light sensitive YtvA protein from Bacillus subtilis
Author(s) -
Buttani Valentina,
Losi Aba,
Polverini Eugenia,
Gärtner Wolfgang
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.06.007
Subject(s) - gtp' , bacillus subtilis , chemistry , biophysics , blue light , guanosine , guanosine diphosphate , flavin group , phytochrome , fluorescence , biochemistry , binding site , guanosine triphosphate , binding domain , biology , enzyme , bacteria , red light , physics , botany , quantum mechanics , optics , genetics
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 (GTP TR ) 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 GTP TR , suggesting that light‐driven conformational changes are transmitted from the LOV core to the GTP TR 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.