Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 403, Issue 1, Pages 78-87Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2010.08.036
Keywords
YtvA; photoreceptor; SAXS; AUC; oligomerization state
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Funding
- Leibniz-institut fir Molekulare Pharmakologie
- Deutsche Forschungsgemeinschaft [SCHM880/8-1]
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Photoreceptors play an important role in plants and bacteria by converting extracellular stimuli into intracellular signals. One distinct class are the blue-light-sensitive phototropins harboring a light oxygen voltage (LOV) domain coupled to various effector domains. Photon absorption by the chromophore within the LOV domain results in an activation of the output domain via mechanisms that are hitherto not well understood. The photoreceptor YtvA from Bacillus subtilis is a bacterial analog of phototropins, consists of an LOV and a sulfate transporter/anti-sigma factor antagonist domain, and is involved in the response of the bacterium to environmental stress. We present here analytical ultracentrifugation studies and small-angle X-ray scattering experiments, showing that YtvA is a dimer. On the basis of these results, we present a low-resolution model of the dimer in the dark and the lit state of the protein. In addition, we show that YtvA does not change its oligomerization state or its overall shape upon light activation. (C) 2010 Elsevier Ltd. All rights reserved.
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