S27, S30, S274, S300, S317, S325, S332, and S349 of the PHOT1a sequence of Avena sativa
First-pass extracted concept
PHOT1a phototropin 1 from Avena sativa
Aliases
PHOT1a, phototropin 1
Evidence Snippets
Supporting Sources
Linked Claims
In Avena sativa PHOT1a, the N-terminus upstream of LOV1 and the hinge region between LOV1 and LOV2 are autophosphorylation regions.
We describe here two additional domains, the N-terminus upstream of LOV1 and the hinge region between LOV1 and LOV2, as the regions for autophosphorylation
Protein kinase A phosphorylation of recombinant phototropin domains had the same site specificity as the phototropin kinase.
phosphorylation of recombinant domains by protein kinase A, which turned out to have the same site specificity as the phototropin kinase
In vivo, serines close to the LOV1 domain are phosphorylated at lower blue-light fluence than serines close to the LOV2 domain.
Investigation of the autophosphorylation in vivo revealed that serines close to the LOV1 domain are phosphorylated at lower fluence of blue light than the serines close to the LOV2 domain.
Recovery of phosphorylation in vivo during a dark period after saturating irradiation is caused by dephosphorylation rather than by degradation of phosphorylated phototropin and new synthesis of nonphosphorylated phototropin.
Recovery of phosphorylation in vivo during a dark period after saturating irradiation is caused by dephosphorylation rather than by degradation of the phosphorylated form and new synthesis of nonphosphorylated phototropin.
The autophosphorylation sites in Avena sativa PHOT1a were identified as S27, S30, S274, S300, S317, S325, S332, and S349.
the phosphorylation sites were identified by site-directed mutagenesis as S27, S30, S274, S300, S317, S325, S332, and S349 of the PHOT1a sequence of Avena sativa