Oligomeric structure of LOV domains in Arabidopsis phototropin.
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.
Katsura
Hitomi
H
Department of Biological Science, Graduate School of Science, Osaka Prefecture University, Naka-ku, Sakai, Osaka, Japan.
Zikihara
Kazunori
K
Okajima
Koji
K
Yoshihara
Shizue
S
Tokutomi
Satoru
S
D017360:Arabidopsis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002942:Circular Dichroism; D055503:Protein Multimerization; D017433:Protein Structure, Secondary
D029681:Arabidopsis Proteins