Here we report that histidine substitution of Arg-472 located within the A'α-helix of Arabidopsis phot1 constitutively activates phot1 kinase activity in vitro without affecting LOV2 photochemistry.
First-pass extracted concept
Arabidopsis phototropin 1 R472H variant
Aliases
Arabidopsis phot1 R472H, phot1 R472H
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The Arabidopsis phot1 R472H variant constitutively activates phot1 kinase activity in vitro without affecting LOV2 photochemistry.
Here we report that histidine substitution of Arg-472 located within the A'α-helix of Arabidopsis phot1 constitutively activates phot1 kinase activity in vitro without affecting LOV2 photochemistry.
In a phot-deficient mutant background, phot1 R472H is autophosphorylated in darkness in vivo but cannot initiate phot1 signaling in the absence of light.
Expression analysis of phot1 R472H in the phot-deficient mutant confirmed that it is autophosphorylated in darkness in vivo but unable to initiate phot1 signaling in the absence of light.
phot1 R472H is poorly functional under low-light conditions but can restore phototropism, chloroplast accumulation, stomatal opening, and leaf positioning and expansion at higher light intensities.
Instead, we found that phot1 R472H is poorly functional under low-light conditions but can restore phototropism, chloroplast accumulation, stomatal opening, and leaf positioning and expansion at higher light intensities.
The activity of phot1 R472H under high-light conditions may be attributable to additional increases in LOV2-mediated photoreceptor autophosphorylation.
whereas the activity of the mutant under high-light conditions can be attributed to additional increases in LOV2-mediated photoreceptor autophosphorylation.
The elevated phosphorylation status of the phot1 R472H mutant may be partly accommodated in Arabidopsis by reduced mutant stability.
Our findings suggest that Arabidopsis can adapt to the elevated phosphorylation status of the phot1 R472H mutant in part by reducing its stability