Abstract
The plant Shewanella-like PPP protein phosphatases, SLP1 and SLP2, are localized to the chloroplast and mitochondria, respectively. Originally uncovered through bioinformatics, these enzymes have been proven to be bona fide protein serine/threonine phosphatases that originated in bacteria but display limited distribution across eukaryotes. They are remarkably conserved in plants, suggesting they play fundamental roles in plant chloroplast and mitochondrial biology. SLP1 appears to reside in the stromal or soluble fraction of chloroplasts and is not expressed in non-photosynthetic plastids. SLP2 is found in peroxisomes but is predominately localized to mitochondria and specifically in the mitochondrial intermembrane space. Like many proteins destined for the mitochondrial intermembrane space, SLP2 is retained here by the formation of disulfide bonds generated by association with oxidoreductase Mia40. We review the unique aspects of these plant enzymes and discuss the use of quantitative mass spectrometry (MS) to discover protein phosphatase substrates.
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Johnson, J.J., White-Gloria, C., Toth, R., Labandera, AM., Uhrig, R.G., Moorhead, G.B. (2020). SLP1 and SLP2: Ancient Chloroplast and Mitochondrial Protein Phosphatases. In: Pandey, G.K. (eds) Protein Phosphatases and Stress Management in Plants. Springer, Cham. https://doi.org/10.1007/978-3-030-48733-1_1
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DOI: https://doi.org/10.1007/978-3-030-48733-1_1
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