Structure and function of a short LOV protein from the marine phototrophic bacterium Dinoroseobacter shibae

• DOI: 10.1186/s12866-015-0365-0
• Publication Date: 2015-02-13T07:24:41Z
• Authors: Stephan Endres; Joachim Granzin; Franco Circolone; Andreas Stadler; Ulrich Krauss; Thomas Drepper; Vera Svensson; Esther Knieps-Grü...; Astrid Wirtz; Anneliese Cousin; Petra Tielen; Dieter Willbold; Karl-Erich Jaeger; Renu Batra-Saffer...
• Keywords: PAS domain; Chromophore

Light, oxygen, voltage (LOV) domains are widely distributed in plants, algae, fungi, bacteria, and represent the photo-responsive of various blue-light photoreceptor proteins. Their photocycle involves triggered adduct formation between C(4a) atom a non-covalently bound flavin chromophore sulfur conserved cysteine LOV sensor domain. proteins show considerable variation structure N- C-terminal elements which flank core domain, as well lifetime state. Here, we report photochemical, structural functional characterization DsLOV, protein from photoheterotrophic marine α-proteobacterium Dinoroseobacter shibae exhibits an average state 9.6 s at 20°C, thus represents fastest reverting bacterial reported so far. Mutational analysis D. revealed unique role DsLOV controlling induction photopigment synthesis absence blue-light. The dark crystal determined 1.5 Å resolution reveals domain with extended N-terminal cap. dimer interface forms network hydrogen bonds involving residues N-terminus β-scaffold photoexcited suggests increased flexibility N-cap region significant shift Cα backbone β strands ends results presented here cover unusual short including its regulatory function, extremely fast recovery mediated interface. Due to photophysical, properties, might serve alternative model system for studying light perception by physiological responses bacteria.