Mild proteasomal stress improves photosynthetic performance in Arabidopsis chloroplasts
Julia Grimmer,
Stefan Helm,
Dirk Dobritzsch,
Gerd Hause,
Gerta Shema,
René P. Zahedi and
Sacha Baginsky ()
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Julia Grimmer: Martin-Luther-University Halle-Wittenberg
Stefan Helm: Martin-Luther-University Halle-Wittenberg
Dirk Dobritzsch: Martin-Luther-University Halle-Wittenberg
Gerd Hause: Biocenter of the University, Martin-Luther-University Halle-Wittenberg
Gerta Shema: Leibniz-Institut für Analytische Wissenschaften -ISAS- e.V.
René P. Zahedi: Leibniz-Institut für Analytische Wissenschaften -ISAS- e.V.
Sacha Baginsky: Martin-Luther-University Halle-Wittenberg
Nature Communications, 2020, vol. 11, issue 1, 1-11
Abstract:
Abstract The proteasome is an essential protein-degradation machinery in eukaryotic cells that controls protein turnover and thereby the biogenesis and function of cell organelles. Chloroplasts import thousands of nuclear-encoded precursor proteins from the cytosol, suggesting that the bulk of plastid proteins is transiently exposed to the cytosolic proteasome complex. Therefore, there is a cytosolic equilibrium between chloroplast precursor protein import and proteasomal degradation. We show here that a shift in this equilibrium, induced by mild genetic proteasome impairment, results in elevated precursor protein abundance in the cytosol and significantly increased accumulation of functional photosynthetic complexes in protein import-deficient chloroplasts. Importantly, a proteasome lid mutant shows improved photosynthetic performance, even in the absence of an import defect, signifying that functional precursors are continuously degraded. Hence, turnover of plastid precursors in the cytosol represents a mechanism to constrain thylakoid membrane assembly and photosynthetic electron transport.
Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15539-8
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DOI: 10.1038/s41467-020-15539-8
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