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Tandem mass-spectrometry identifies sites of 3 posttranslational modifications of spinach light-harvesting chlorophyll protein-II - proteolytic cleavage, acetylation, and phosphorylation

Academic Article
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Overview

authors

  • Michel, H.
  • Griffin, Patrick
  • Shabanowitz, J.
  • Hunt, D. F.
  • Bennett, J.

publication date

  • September 1991

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The photosynthetic membranes of spinach (Spinacia oleracea L.) chloroplasts were incubated with [gamma-32P] ATP. When the thylakoid membrane kinase was activated with light, the 25- and 27-kDa forms of the light-harvesting chlorophyll a/b protein (LHC II) were phosphorylated on their amino termini. Treatment of the membranes with proteinase K or thermolysin released phosphopeptides which were purified by ferric ion affinity chromatography and reverse phase high performance liquid chromatography. Sequencing of the phosphopeptides was performed with tandem quadrupole mass spectrometry. Three different phosphopeptides Ac-RKTAGKPKT, Ac-RKTAGKPKN, and Ac-RKSAGKPKN originating from class I LHC II were examined after release by thermolysin. One phosphopeptide, Ac-RRTVKSAPQ, originating from class II LHC II was examined after release by proteinase K. Each of the four LHC II phosphopeptides was derived from the amino terminus of a distinct protein. Peptides were acetylated at their amino-terminal arginine and were phosphorylated on either threonine or serine in the third position. We conclude that proteolytic processing of pre-LHC II occurs at a conserved methionyl-arginyl bond and is followed by amino-terminal acetylation of the arginine and nearby phosphorylation of the mature LHC II. Eight different peptides were synthesized in acetylated and nonacetylated forms as substrates for the thylakoid membrane kinase. From a comparison of the kinetics of phosphate incorporation into the peptides, we conclude that basic residues on both sides of the phosphorylation site are important for enzyme recognition. Acetylation of the amino terminus is not required for phosphorylation.

subject areas

  • Acetylation
  • Amino Acid Sequence
  • Amino Acids
  • Chromatography, High Pressure Liquid
  • Hydrolysis
  • Light-Harvesting Protein Complexes
  • Mass Spectrometry
  • Molecular Sequence Data
  • Phosphorylation
  • Photosynthetic Reaction Center Complex Proteins
  • Plants
  • Protein Processing, Post-Translational
  • Substrate Specificity
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 1894641
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Additional Document Info

start page

  • 17584

end page

  • 17591

volume

  • 266

issue

  • 26

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