Forests

Introduction

Protein phosphorylation orchestrates a plethora of cellular processes in eukaryotes, including the fine-tuning of photosynthesis in response to environmental changes. Thylakoid protein phosphorylation, responsible for modulating photosystem dynamics and acclimation to light conditions, is an intricate system within chloroplasts. In a recent study published in Plant Physiology, Gerotto et al. have dissected the role of SERINE/THREONINE PROTEIN KINASE STN8 in this process by examining a mutant moss, Physcomitrella patens, which lacks the STN8 gene compared to its presence in Arabidopsis thaliana. This comparative approach sheds light on variances across phylogenetic lines and the evolution of photosynthetic regulatory mechanisms.

Keywords

1. Thylakoid Protein Phosphorylation
2. Moss Photosynthesis Regulation
3. STN8 Protein Kinase
4. Physcomitrella patens Photosystem
5. Chloroplast Acclimation Process

Eukaryotic organisms rely on protein phosphorylation to regulate vital processes, particularly the acclimation of photosynthesis to environmental inputs. The conserved regulatory mechanism within chloroplasts, thylakoid protein phosphorylation, has shown diverse patterns in various phylogenetic groups. In a recent study published in the journal Plant Physiology, researchers from the Department of Biochemistry, Molecular Plant Biology of the University of Turku, along with collaborators from the University of Padova, have made strides in understanding these differences. The study, titled “Thylakoid Protein Phosphorylation Dynamics in a Moss Mutant Lacking SERINE/THREONINE PROTEIN KINASE STN8” (DOI: 10.1104/pp.19.00117), presents an analysis of thylakoid protein phosphorylation in the moss Physcomitrella patens, contrasting its response to the well-characterized higher plant Arabidopsis thaliana.

This plant physiology research, funded in part by non-U.S. government grants, zeros in on a moss (P. patens) that lacks the kinase STN8, a protein responsible for the phosphorylation of certain components within the thylakoid membrane. It is within this membrane that photosynthesis, a crucial process by which plants convert light energy into chemical energy, operates.

In Arabidopsis and other higher plants, STN8 has a specific role in the phosphorylation of photosystem II core proteins, a key step in the repair and regulation of photosynthetic activity. Examining the stn8 lacking mutant of P. patens has provided significant insights into the role of STN8 in the moss and potential evolutionary implications.

The study began with a detailed characterization of the thylakoid phosphoproteome in P. patens using state-of-the-art microscopy, including electron transmission microscopy, and various biochemical analysis methods. The research team, including Caterina Gerotto, Andrea Trotta, Azfar Ali Bajwa, Ilaria Mancini, Tomas Morosinotto, and Eva-Mari Aro, revealed that the absence of STN8 affects the dynamics of the thylakoid membrane proteins, specifically in how they react to changes in light intensity.

Light Harvesting Under the Microscope

Light harvesting in plants involves a complex interplay of proteins that work in concert to absorb light and channel energy into the photosynthetic reaction centers. The phosphorylation state of these proteins is a crucial regulatory mechanism that helps plants respond to varying light conditions. In the absence of STN8, the study found that P. patens modifies its light-harvesting protein complexes differently from A. thaliana.

In previous studies, phosphorylation of light-harvesting complex II (LHCII) was shown to be a key element in adjusting the light-harvesting function in plants. Specifically, STN8 kinase activity has been implicated in the reversible phosphorylation of CP29, a component of LHCII, as part of the protective response to high light in higher plants. However, P. patens, despite lacking STN8, displays an adaptive light-harvesting mechanism that is functional but fundamentally dissimilar to that of higher plants.

The Role of Thylakoid Architecture

The architecture of the thylakoid membrane in plants is a determinant for the efficiency of photosynthesis. The study’s findings suggest that P. patens has evolved distinct structural features and associated phosphorylation patterns to maintain photosynthetic operation in the absence of STN8. The thylakoid membrane in P. patens—a non-vascular plant—lacks the pronounced grana structure found in the chloroplasts of higher plants, which may have profound implications for its protein phosphorylation dynamics and functional organization.

Evolutionary Implications

By comparing the mutant moss lacking STN8 with the well-studied phosphorylation events in A. thaliana, the researchers provide evidence of evolutionary divergence in photosynthetic regulation mechanisms. The present study not only deepens our understanding of the regulatory complexity of thylakoid protein phosphorylation in different organisms but it also raises questions about the evolutionary pressures that led to the development of varying regulatory strategies among photosynthetic eukaryotes.

Furthermore, the analysis paves the way for exploring the evolutionary trajectory of photosynthetic organisms as they transitioned from aquatic to terrestrial habitats. Previous research has postulated that as plants adapted to the land environment, they developed sophisticated mechanisms to cope with the vastly different light and temperature conditions. Gerotto et al.’s study reinforces this hypothesis by suggesting that P. patens and possibly other mosses have evolved unique photosynthetic regulation systems that are independent of STN8 kinase.

Conclusion

This path-opening study by Gerotto et al. not only expands the scientific community’s knowledge of photosynthetic regulation in a relatively understudied non-vascular plant but also underscores the evolutionary significance of protein phosphorylation mechanisms across different species. The absence of STN8 kinase in P. patens and the resultant differences in thylakoid protein phosphorylation dynamics highlight the adaptive plasticity of photosynthetic organisms and the complexity of the light acclimation process.

As researchers continue to delve deeper into the nuances of photosynthetic regulation, such studies are instrumental in identifying potential targets for genetic engineering aimed at enhancing crop productivity and stress resistance. Gerotto et al.’s comprehensive analysis and the utilization of advanced proteomic techniques also set a standard for future research endeavors in plant biology, particularly in examining the impacts of global climate change on the photosynthetic efficiency of diverse plant species.

References

1. Gerotto, C., et al. (2019). Thylakoid Protein Phosphorylation Dynamics in a Moss Mutant Lacking SERINE/THREONINE PROTEIN KINASE STN8. Plant Physiol, 180(3), 1582–1597. DOI: 10.1104/pp.19.00117
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3. Bonardi, V., et al. (2005). Photosystem II core phosphorylation and photosynthetic acclimation require two different protein kinases. Nature, 437, 1179–1182.
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