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Sci. Signal., 2 August 2011
Vol. 4, Issue 184, p. ra50
[DOI: 10.1126/scisignal.2001945]


Editor's Summary

Coming Together in the Light
The filamentous fungus Neurospora crassa uses two blue-light sensors, white collar-1 (WC-1) and VIVID (VVD), both of which contain light, oxygen, or voltage (LOV) domains, to regulate its responses to light. WC-1 and WC-2 form a complex (WCC) to drive expression of light-induced genes, including vvd, whereas VVD tunes responses to light by directly interacting with and antagonizing the function of WCC. Vaidya et al. solved the crystal structure of the light-induced dimer of VVD and compared it to previously determined structures of the dark-state, monomeric protein. This analysis revealed that light not only induced a conformational change in the positioning of the N-terminal cap of one subunit of VVD but also triggered the opening of a binding pocket in the opposing subunit, into which the N-terminal cap could dock. Determining the structure explained the functional responses observed in vvd-deficient Neurospora that expressed variant VVD proteins and may inform mechanisms by which LOV-containing proteins interact.

Citation: A. T. Vaidya, C.-H. Chen, J. C. Dunlap, J. J. Loros, B. R. Crane, Structure of a Light-Activated LOV Protein Dimer That Regulates Transcription. Sci. Signal. 4, ra50 (2011).

Read the Full Text

The Neurospora photoreceptor VIVID exerts negative and positive control on light sensing to achieve adaptation.
E. Gin, A. C. R. Diernfellner, M. Brunner, and T. Hofer (2014)
Mol Syst Biol 9, 667
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