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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 differentiationстатья
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Дата последнего поиска статьи во внешних источниках: 26 июня 2019 г.
- Авторы: Sineshchekov Vitaly, Koppel Larissa, Kim Jeong-Il
- Журнал: Photochemical and Photobiological Sciences
- Том: 18
- Номер: 5
- Год издания: 2019
- Издательство: Royal Society of Chemistry
- Местоположение издательства: United Kingdom
- Первая страница: 1242
- Последняя страница: 1248
- DOI: 10.1039/C8PP00574E
- Аннотация: 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)1. 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)2, 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.
- Добавил в систему: Коппель Лариса Алексеевна