Journal
FEBS LETTERS
Volume 580, Issue 16, Pages 3818-3822Publisher
WILEY
DOI: 10.1016/j.febslet.2006.06.007
Keywords
LOV-proteins; blue-light photoreceptor; GTP-binding proteins; ATP-binding proteins; STAS domain; fluorescence
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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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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