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An activated glutamate residue identified in photosystern II at the interface between the manganese-stabilizing subunit and the D2 polypeptide

Academic Article
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Overview

authors

  • Rexroth, S.
  • Wong, C. C. L.
  • Park, J. H.
  • Yates III, John
  • Barry, B. A.

publication date

  • September 2007

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Photosystem II (PSII) catalyzes the oxidation of water during oxygenic photosynthesis. PSII is composed both of intrinsic subunits, such as D1, D2, and CP47, and extrinsic subunits, such as the manganese-stabilizing subunit (MSP). Previous work has shown that amines covalently bind to amino acid residues in the CP47, D1, and D2 subunits of plant and cyanobacterial PSII, and that these covalent reactions are prevented by the addition of chloride in plant preparations depleted of the 18- and 24-kDa extrinsic subunits. It has been proposed that these reactive groups are carbonyl-containing, post-translationally modified amino acid side chains (Ouellette, A. J. A., Anderson, L. B., and Barry, B. A. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 2204-2209 and Anderson, L. B., Ouellette, A. J. A., and Barry, B. A. (2000) J. Biol. Chem. 275, 4920-4927). To identify the amino acid binding site in the spinach D2 subunit, we have employed a biotin-amine labeling reagent, which can be used in conjunction with avidin affinity chromatography to purify biotinylated peptides from the PSII complex. Multidimensional chromato-graphic separation and multistage mass spectrometry localizes a novel post-translational modification in the D2 subunit to glutamate 303. We propose that this glutamate is activated for amine reaction by post-translational modification. Because the modified glutamate is located at a contact site between the D2 and manganese-stabilizing subunits, we suggest that the modification is important in vivo in stabilizing the interaction between these two PSII subunits. Consistent with this conclusion, mutations at the modified glutamate alter the steady-state rate of photosynthetic oxygen evolution.

subject areas

  • Binding Sites
  • Biological Evolution
  • Carboxylic Acids
  • Crystallography, X-Ray
  • Electrophoresis, Gel, Two-Dimensional
  • Glutamic Acid
  • Manganese
  • Mass Spectrometry
  • Molecular Conformation
  • Mutation
  • Oxygen
  • Photosynthesis
  • Photosystem II Protein Complex
  • Protein Processing, Post-Translational
  • Tyrosine
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M704394200

PubMed ID

  • 17666402
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Additional Document Info

start page

  • 27802

end page

  • 27809

volume

  • 282

issue

  • 38

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