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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© 2011 American Association for the Advancement of Science