Protein transphosphorylation during the mutual interaction between phytochrome a and a nuclear isoform of nucleoside diphosphate kinase is regulated by red light
- Авторы: Hetmann A.1, Wujak M.1, Kowalczyk S.1
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Учреждения:
- Faculty of Biology and Environment Protection, Department of Biochemistry
- Выпуск: Том 81, № 10 (2016)
- Страницы: 1153-1162
- Раздел: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/151043
- DOI: https://doi.org/10.1134/S0006297916100126
- ID: 151043
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Аннотация
The nuclear isoform of nucleoside diphosphate kinase isoenzyme NDPK-In undergoes strong catalytic activation upon its interaction with the active form of phytochrome A (Pfr) in red light. The autophosphorylation or intermolecular transphosphorylation of NDPK-In leads to the formation of phosphoester bonds stable in acidic solution. The phosphate residue of the phosphamide bond in the active center of NDPK-In can also be transferred to serine and threonine residues localized in other proteins, including phytochrome A. Phytochrome A, similarly to NDPK-In, undergoes autophosphorylation on serine and threonine residues and can phosphorylate some potential substrate proteins. The physical interaction between phytochrome A in the Pfr form and NDPK-In results in a significant increase in the kinase activity of NDPK-In. The results presented in this work indicate that NDPK-In may function as a protein kinase regulated by light.
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Об авторах
A. Hetmann
Faculty of Biology and Environment Protection, Department of Biochemistry
Email: mag_wuj@umk.pl
Польша, 1 Lwowska St, Toruń, 87-100
M. Wujak
Faculty of Biology and Environment Protection, Department of Biochemistry
Автор, ответственный за переписку.
Email: mag_wuj@umk.pl
Польша, 1 Lwowska St, Toruń, 87-100
S. Kowalczyk
Faculty of Biology and Environment Protection, Department of Biochemistry
Email: mag_wuj@umk.pl
Польша, 1 Lwowska St, Toruń, 87-100
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