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Protein transphosphorylation during the mutual interaction between phytochrome a and a nuclear isoform of nucleoside diphosphate kinase is regulated by red light

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Abstract

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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Abbreviations

AK:

adenylate kinase

CAT:

catalase

ER:

endoplasmic reticulum

MAP kinase:

mitogen activated protein kinase

MBP:

myelin basic protein

NDPK:

NDP kinase (nucleoside diphosphate kinase)

NDPK-In :

nuclear isoform of NDPK

phy A:

phytochrome A

PIF/PIL:

phytochrome interacting factor/PIF like

PKS1:

phytochrome kinase substrate 1

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Correspondence to M. Wujak.

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Published in Russian in Biokhimiya, 2016, Vol. 81, No. 10, pp. 1427–1438.

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM16-141, August 8, 2016.

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Hetmann, A., Wujak, M. & Kowalczyk, S. Protein transphosphorylation during the mutual interaction between phytochrome a and a nuclear isoform of nucleoside diphosphate kinase is regulated by red light. Biochemistry Moscow 81, 1153–1162 (2016). https://doi.org/10.1134/S0006297916100126

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