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-fight 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.

Blue news: NTP binding properties of the blue-light sensitive YtvA protein from Bacillus subtilis / BUTTANI V; LOSI A; POLVERINI E.; GARTNER W. - In: FEBS LETTERS. - ISSN 0014-5793. - 580:16(2006), pp. 3818-3822. [10.1016/j.febslet.2006.06.007]

Blue news: NTP binding properties of the blue-light sensitive YtvA protein from Bacillus subtilis.

LOSI, Aba;POLVERINI, Eugenia;
2006

Abstract

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-fight 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.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11381/1510132
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