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Submitted on May 30, 2003
Linköping University, Linköping SE-581 85
Corresponding Author: aleve{at}ibk.liu.se
The proteins in plant photosynthetic thylakoid membranes undergo light-induced phosphorylation but only few phosphoproteins have been characterized. To access the unknown sites of in vivo protein phosphorylation the thylakoid membranes were isolated from Arabidopsis thaliana grown at normal light and the surface exposed peptides were cleaved from the membranes by trypsin. The peptides were methylated, subjected to immobilized metal affinity chromatography and the enriched phosphopeptides were sequenced using tandem nanospray-quadropole-time-of-flight mass spectrometry. Three new phosphopeptides were revealed in addition to the five known phosphorylation sites in photosystem II proteins. All phosphopeptides are found phosphorylated at threonine residues implementing a strict threonine specificity of the thylakoid kinases. For the first time protein phosphorylation is found in photosystem I. The phosphorylation site is localized to the first threonine in the N-terminus of PsaD protein assisting in the electron transfer from photosystem I to ferredoxin. A new phosphorylation site is also revealed in the acetylated N-terminus of the minor chlorophyll a binding protein CP29. The third novel phosphopeptide of 25 amino acids belongs to a nuclear encoded protein annotated as “expressed protein” in Arabidopsis database. The protein precursor has a chloroplast targeting peptide followed by the mature protein with two trans-membrane helices and a molecular mass of 14 kDa. This previously uncharacterized protein is named Thylakoid Membrane Phosphoprotein of 14 kDa (TMP14). The finding of the novel phosphoproteins extends involvement of the redox-regulated protein phosphorylation in photosynthetic membranes beyond the photosystem II and its light-harvesting antennae.
Revised on July 26, 2003
Accepted on July 26, 2003
Identification of three previously unknown in vivo protein phosphorylation sites in thylakoid membranes of Arabidopsis thaliana
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