Oligomeric structure of LOV domains in Arabidopsis phototropin

FEBS Lett. 2009 Feb 4;583(3):526-30. doi: 10.1016/j.febslet.2009.01.019. Epub 2009 Jan 21.

Abstract

Oligomeric structures of the four LOV domains in Arabidopsis phototropin1 (phot1) and 2 (phot2) were studied using crosslinking. Both LOV1 domains of phot1 and phot2 form a dimer independently on the light conditions, suggesting that the LOV1 domain can be a stable dimerization site of phot in vivo. In contrast, phot1-LOV2 is in a monomer-dimer equilibrium and phot2-LOV2 exists as a monomer in the dark. Blue light-induced a slight increase in the monomer population in phot1-LOV2, suggesting a possible blue light-inducible dissociation of dimers. Furthermore, blue light caused a band shift of the phot2-LOV2 monomer. CD spectra revealed the unfolding of helices and the formation of strand structures. Both light-induced changes were reversible in the dark.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / chemistry*
  • Arabidopsis / genetics
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / chemistry*
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Circular Dichroism
  • Protein Multimerization
  • Protein Structure, Secondary

Substances

  • Arabidopsis Proteins