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A CK2 site is reversibly phosphorylated in the photosystem II subunit CP29
Author(s) -
Testi Maria Grazia,
Croce Roberta,
Laureto Patrizia Polverino-De,
Bassi Roberto
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01333-6
Subject(s) - photosystem ii , protein subunit , phosphorylation , chemistry , photosystem i , biophysics , biochemistry , biology , photosynthesis , gene
Protein phosphorylation is a major mechanism in the regulation of protein function. In chloroplast thylakoids several photosystem II subunits, including the major antenna light‐harvesting complex II and several core complex components, are reversibly phosphorylated depending on the redox state of the electron carriers. A previously unknown reversible phosphorylation event has recently been described on the CP29 subunit which leads to conformational changes and protection from cold stress (Bergantino, E., Dainese, P., Cerovic, Z. Sechi, S. and Bassi, R. (1995) J. Biol Chem . 270, 8474–8481). In this study, we have identified the phosphorylation site on the N‐terminal, stroma‐exposed domain, showing that it is located in a sequence not homologous to the other members of the Lhc family. The phosphorylated sequence is unique in chloroplast membranes since it meets the requirements for CK2 (casein kinase II) kinases. The possibility that this phosphorylation is involved in a signal transduction pathway is discussed.