title: Protein Transphosphorylation During the Mutual Interaction between Phytochrome A and a Nuclear Isoform of Nucleoside Diphosphate Kinase Is Regulated by Red Light.
abstract: The nuclear isoform of nucleoside diphosphate kinase isoenzyme NDPK-Inundergoes strong catalytic activation upon its interaction with the active form of phytochrome A (Pfr) in red light. The autophosphorylation or intermolecular transphosphorylation of NDPK-Inleads to the formation of phosphoester bonds stable in acidic solution. The phosphate residue of the phosphamide bond in the active center of NDPK-Incan 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-Inresults in a significant increase in the kinase activity of NDPK-In. The results presented in this work indicate that NDPK-Inmay function as a protein kinase regulated by light.
authors.affiliation: Nicolaus Copernicus University, Faculty of Biology and Environment Protection, Department of Biochemistry, Toruń 87-100, Poland. mag_wuj@umk.pl.
authors.forename: A
authors.initials: A
authors.lastname: Hetmann
authors.forename: M
authors.initials: M
authors.lastname: Wujak
authors.forename: S
authors.initials: S
authors.lastname: Kowalczyk
mesh_terms: D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D008027:Light; D009701:Nucleoside-Diphosphate Kinase / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation / Q000235:genetics / Q000528:radiation effects; D051942:Phytochrome A / Q000235:genetics / Q000378:metabolism*
chemical_list: D029681:Arabidopsis Proteins; D051942:Phytochrome A; D009701:Nucleoside-Diphosphate Kinase