Residues Clustered in the Light-Sensing Knot of Phytochrome B are Necessary for Conformer-Specific Binding to Signaling Partner PIF3

DOI

Bibliographic Information

Other Title
  • Phytochrome BのN末端領域内の結び目構造はPIF3との相互作用に関わる

Abstract

PHYTOCHROME INTERACTING FACTOR 3 (PIF3) interacts with the active phytochrome B (phyB). To identify mutations in the phyB N-terminus that disrupt this interaction, we developed a yeast reverse-hybrid screen. Fifteen mutations identified in this screen, or in previous genetic screens for Arabidopsis mutants showing reduced sensitivity to red light, were shown to disrupt light-induced binding of phyB to PIF3 in in vitro binding assays. These phyB mutations fall into two classes: Class I (11 mutations) containing those defective in light perception, and Class II (4 mutations) containing those normal in light perception, but defective in binding to PIF3. A bioinformatics comparison of phyB to BphP, for which a crystal structure has been solved, predicts that three of the four Class II mutated residues are solvent exposed in a cleft between PAS and GAF domains, suggesting that these residues could be directly required for the physical interaction of phyB with PIF3.

Journal

Details 詳細情報について

  • CRID
    1390001205632530560
  • NII Article ID
    130006994270
  • DOI
    10.14841/jspp.2009.0.0288.0
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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