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Submitted on August 21, 2001
Chemistry, UCLA, Los Angeles, CA 90095
Corresponding Author: jpw{at}chem.ucla.edu
Proteomics seeks to address the entire complement of an organism’s protein gene-products but experimental analysis of such complex mixtures is biased against low abundance and membrane proteins. Electrospray-ionization mass spectrometry coupled with reverse-phase chromatography was used to separate and catalogue all detectable proteins in samples of photosystem II (PS II) enriched thylakoid membrane sub-domains (grana) from pea and spinach. Around ninety intact mass tags were detected corresponding to approximately forty gene products with variable post-translational covalent modifications. Provisional identity of thirty of these gene products was proposed based upon coincidence of measured mass with that calculated from genomic sequence. Analysis of isolated PS II complexes allowed detection and resolution of a minor population of D1 (PsbA) that was apparently palmitoylated and not detected in less purified preparations. Based upon observed +80 Da adducts, D1, D2 (PsbD), CP43 (PsbC), 2 Lhcb’s and PsbH were confirmed to be phosphorylated and a new phosphoprotein was proposed to be the product of psbT. The appearance of a second +80 Da adduct on PsbH provides direct evidence for a second phosphorylation site on PsbH, complicating interpretation of its role in regulation of thylakoid membrane organization and function, including light State-transitions. Adducts of +32 Da, presumably arising from oxidative modification during illumination, were associated with more highly phosphorylated forms of PsbH implying a relationship between the two phenomena. Intact mass proteomics of organellar sub-fractions and more highly purified protein complexes provides increasingly detailed insights into functional genomics of photosynthetic membranes.
Revised on October 11, 2001
Accepted on October 12, 2001
The chloroplast grana proteome difined by intact mass measurements from LC-MS
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