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REVIEW article
Front. Plant Sci.
Sec. Aquatic Photosynthetic Organisms
Volume 16 - 2025 |
doi: 10.3389/fpls.2025.1540914
The regulatory impact of serine/threonine-specific protein phosphorylation among cyanobacteria
Provisionally accepted
Martin Hagemann *
Thomas Barske - Institute of Biosciences, University of Rostock, Rostock, Germany
Cyanobacteria are the only prokaryotes capable of performing oxygenic photosynthesis. To thrive under environmental fluctuations, photosynthesis and metabolic activities needs to be adjusted.Previous studies showed that the acclimation of primary carbon metabolism to fluctuating carbon/nitrogen levels is mainly regulated at post-transcriptional level including diverse posttranslational modifications (PTMs). Protein phosphorylation is regarded as main PTM in the sensing and balancing metabolic changes. In this review we aim to summarize the knowledge on serine/threonine-specific protein phosphorylation among cyanobacteria. Phosphoproteome studies identified several hundred phosphoproteins bearing many more specific phosphorylation sites. On the other hand, only relatively few serine/threonine-specific protein kinases were annotated in cyanobacterial genomes, for example 12 in the model cyanobacterium Synechocystis sp. PCC 6803. Systematic mutation of the kinase-encoding genes revealed first insights into their specific functions and substrates. Future research is needed to address how a limited number of protein kinases can specifically modify hundreds of phosphoproteins and to uncover their roles in the regulatory networks of cyanobacterial metabolism.
Keywords: Synechocystis, Proteomics, kinase, mutant, environment
Received: 06 Dec 2024; Accepted: 22 Jan 2025.
Copyright: © 2025 Hagemann and Barske. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence:
Martin Hagemann, Institute of Biosciences, University of Rostock, Rostock, D-18059, Germany
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