z-logo
Premium
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom