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Sci. Signal., 2 August 2011
[DOI: 10.1126/scisignal.2001945]

Supplementary Materials for:

Structure of a Light-Activated LOV Protein Dimer That Regulates Transcription

Anand T. Vaidya, Chen-Hui Chen, Jay C. Dunlap, Jennifer J. Loros, Brian R. Crane*

*To whom correspondence should be addressed. E-mail: bc69{at}cornell.edu

This PDF file includes:

  • Fig. S1. VVD-II has a high redox potential.
  • Fig. S2. Comparison of the LSD structure of VVD with time-resolved SAXS data.
  • Fig. S3. Targeting the cross-linking ability of the LSD of VVD.
  • Fig. S4. The csr-1 knock-in strains used in this study were homokaryons.
  • Fig. S5. Light-dependent induction of vvd expression and VVD protein production in strains with various vvd mutant alleles.
  • Fig. S6. Sequence similarity between VVD and WC-1.
  • Fig. S7. Comparison of the light-induced changes in hydrogen bonding found for VVD and the A. sativa phototropin LOV2 domain.
  • Table S1. Data collection and phasing statistics.
  • Table S2. Conservation of light-dependent signaling and dimerization in the fungal LOV domains.
  • Reference

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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).

© 2011 American Association for the Advancement of Science


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