First-pass extracted concept

Arabidopsis phototropin 1 R472H variant

Candidate: toolkit item1 source documents5 linked claims
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Aliases

Arabidopsis phot1 R472H, phot1 R472H

Evidence Snippets

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.
Evidence 1Source 1DOIPubMedprovenance

Supporting Sources

Linked Claims

Claim 1activity changesupports2017Source 1DOIPubMed

The Arabidopsis phot1 R472H variant constitutively activates phot1 kinase activity in vitro without affecting LOV2 photochemistry.

Quoted textsource-backed
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.
Claim 2autophosphorylation statesupports2017Source 1DOIPubMed

In a phot-deficient mutant background, phot1 R472H is autophosphorylated in darkness in vivo but cannot initiate phot1 signaling in the absence of light.

Quoted textsource-backed
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.
Claim 3light condition dependencesupports2017Source 1DOIPubMed

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.

Quoted textsource-backed
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.
Claim 4mechanistic interpretationsupports2017Source 1DOIPubMed

The activity of phot1 R472H under high-light conditions may be attributable to additional increases in LOV2-mediated photoreceptor autophosphorylation.

Quoted textsource-backed
whereas the activity of the mutant under high-light conditions can be attributed to additional increases in LOV2-mediated photoreceptor autophosphorylation.
Claim 5stability interpretationsupports2017Source 1DOIPubMed

The elevated phosphorylation status of the phot1 R472H mutant may be partly accommodated in Arabidopsis by reduced mutant stability.

Quoted textsource-backed
Our findings suggest that Arabidopsis can adapt to the elevated phosphorylation status of the phot1 R472H mutant in part by reducing its stability