Lysine acetylation regulates moonlighting activity of the <scp>E2</scp> subunit of the chloroplast pyruvate dehydrogenase complex in <i>Chlamydomonas</i>

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  • Daniel Neusius
    Molecular Plant Sciences, Faculty of Biology LMU Munich Großhaderner Str. 2‐4, 82152 Planegg‐ Martinsried Germany
  • Laura Kleinknecht
    Molecular Plant Sciences, Faculty of Biology LMU Munich Großhaderner Str. 2‐4, 82152 Planegg‐ Martinsried Germany
  • Jing Tsong Teh
    Molecular Plant Sciences, Faculty of Biology LMU Munich Großhaderner Str. 2‐4, 82152 Planegg‐ Martinsried Germany
  • Matthias Ostermeier
    Molecular Plant Sciences, Faculty of Biology LMU Munich Großhaderner Str. 2‐4, 82152 Planegg‐ Martinsried Germany
  • Simon Kelterborn
    Experimental Biophysics, Institute of Biology Humboldt University of Berlin Invalidenstr. 42 10115 Berlin Germany
  • Jürgen Eirich
    Institute of Plant Biology and Biotechnology University of Muenster Schlossplatz 7 48149 Münster Germany
  • Peter Hegemann
    Experimental Biophysics, Institute of Biology Humboldt University of Berlin Invalidenstr. 42 10115 Berlin Germany
  • Iris Finkemeier
    Institute of Plant Biology and Biotechnology University of Muenster Schlossplatz 7 48149 Münster Germany
  • Alexandra‐Viola Bohne
    Molecular Plant Sciences, Faculty of Biology LMU Munich Großhaderner Str. 2‐4, 82152 Planegg‐ Martinsried Germany
  • Jörg Nickelsen
    Molecular Plant Sciences, Faculty of Biology LMU Munich Großhaderner Str. 2‐4, 82152 Planegg‐ Martinsried Germany

Description

<jats:title>SUMMARY</jats:title><jats:p>The dihydrolipoamide acetyltransferase subunit DLA2 of the chloroplast pyruvate dehydrogenase complex (cpPDC) in the green alga <jats:italic>Chlamydomonas reinhardtii</jats:italic> has previously been shown to possess moonlighting activity in chloroplast gene expression. Under mixotrophic growth conditions, DLA2 forms part of a ribonucleoprotein particle (RNP) with the <jats:italic>psbA</jats:italic> mRNA that encodes the D1 protein of the photosystem II (PSII) reaction center. Here, we report on the characterization of the molecular switch that regulates shuttling of DLA2 between its functions in carbon metabolism and D1 synthesis. Determination of RNA‐binding affinities by microscale thermophoresis demonstrated that the E3‐binding domain (E3BD) of DLA2 mediates <jats:italic>psbA</jats:italic>‐specific RNA recognition. Analyses of cpPDC formation and activity, as well as RNP complex formation, showed that acetylation of a single lysine residue (K197) in E3BD induces the release of DLA2 from the cpPDC, and its functional shift towards RNA binding. Moreover, Förster resonance energy transfer microscopy revealed that <jats:italic>psbA</jats:italic> mRNA/DLA2 complexes localize around the chloroplast's pyrenoid. Pulse labeling and D1 re‐accumulation after induced PSII degradation strongly suggest that DLA2 is important for D1 synthesis during <jats:italic>de novo</jats:italic> PSII biogenesis.</jats:p>

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