251. The dephosphorylated S8A and S18A mutants of (oat) phytochrome A comprise its two species, phyA' and phyA'', suggesting that autophosphorylation at these sites is not involved in the phyA differentiation.
- Author
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Sineshchekov V, Koppel L, and Kim JI
- Subjects
- Avena growth & development, Avena metabolism, Mutation, Phosphorylation, Phytochrome A genetics, Serine genetics, Avena chemistry, Phytochrome A metabolism, Serine metabolism
- Abstract
Phytochrome A (phyA) is represented in plants by two species, phyA' and phyA'', with different properties and modes of action (Sineshchekov, Funct. Plant Biol., 2019, 46, 118-135). They differ by the modification of a serine(s) residue at the N-terminus, possibly, by phosphorylation. To verify if these serines could be the Ser8 and Ser18 (in Avena sativa phyA, AsphyA), whose autophosphorylation modulates AsphyA stability and sensitivity as shown with the use of the serine-to-alanine substitution AsphyA mutants (S8A, S18A and S8/18A) (Han et al., Plant Cell Physiol., 2010, 51, 596-609), we have undertaken low-temperature (85 K) fluorescence investigations of phyA in these transgenic lines. The content and proportion of phyA' and phyA'' were essentially the same in wild-type AsphyA and its mutants, and in endogenous Arabidopsis phyA. All the lines revealed a higher phyA'/phyA'' proportion upon longer germination-inducing preillumination (3 h vs. 15 min white light) supporting our earlier finding that the phyA differentiation into the subpools is light-regulated. These observations and our earlier data imply that this process involves N-terminal serine(s) different from the autophosphorylated Ser8 and Ser18 (in AsphyA) narrowing down the area of further search for the exact site(s) of the phyA modification.
- Published
- 2019
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