Evidence for a post-translational modification, aspartyl aldehyde, in a photosynthetic membrane protein

Journal of the American Chemical Society
Lorraine B AndersonBridgette A Barry

Abstract

In oxygenic photosynthesis, photosystem II (PSII) carries out the oxidation of water and reduction of plastoquinone. Three PSII subunits contain reactive groups that covalently bind amines and phenylhydrazine. It has been proposed that these reactive groups are carbonyl-containing, co- or post-translationally modified amino acids. To identify modified amino acid residues in one of the PSII subunits (CP47), tandem mass spectrometry was performed. Modified residues were affinity-tagged with either biotin-LC-hydrazide or biocytin hydrazide, which are known to label carbonyl groups. The affinity-tagged subunit was isolated by denaturing gel electrophoresis, and tryptic peptides were then subjected to affinity purification and tandem mass spectrometry. This procedure identified a hydrazide-labeled peptide, which has the sequence XKEGR. This result is supported by quantitative results acquired from peptide mapping and methylamine labeling. The gene sequence and these tandem data predict that the first amino acid, X, which is labeled with the hydrazide reagent, is a modified form of aspartic acid. On the basis of these data, we propose that D348 of the CP47 subunit is post- or co-translationally modified to give a novel amino acid sid...Continue Reading

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Citations

Apr 30, 2011·The Journal of Biological Chemistry·Tina M DreadenBridgette A Barry
May 30, 2009·Biochimica Et Biophysica Acta·Saber Hamdani, Robert Carpentier
Jun 1, 2016·Frontiers in Plant Science·Daniel A WeiszHimadri B Pakrasi
Dec 5, 2014·Journal of the American Chemical Society·Claudia E MurarJeffrey W Bode
Sep 15, 2006·The Journal of Physical Chemistry. a·P ThanasekaranKuang-Lieh Lu

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