ArticlePhotosynthesis research2021
Proximity-based proteomics reveals the thylakoid lumen proteome in the cyanobacterium Synechococcus sp. PCC 7002.
Article in Photosynthesis research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Carbon dioxide concentration alters cyanobacterial carboxysome encapsulation and redox state in Synechococcus sp. PCC 7002.Communications biology · 2026Article
- [COResearch square · 2026Article
- From photosynthetic electron flow to gene regulation: redox signal transduction in cyanobacteria.FEMS microbiology reviews · 2026Review
- Identification of common genes associated with diabetic nephropathy and diabetic retinopathy.Frontiers in cell and developmental biology · 2026Article
- Proximity-based proteomics reveals subcellular targeting sequence in Cyanobacteria.Plant physiology · 2025Article
- Spatial proteomics reveals signal sequence characteristics correlated with localization in cyanobacteria.Plant physiology · 2025Article
- A phase-separated CO2-fixing pyrenoid proteome determined by TurboID in Chlamydomonas reinhardtii.The Plant cell · 2023Article
- Cyanobacterial Algal Bloom Monitoring: Molecular Methods and Technologies for Freshwater Ecosystems.Microorganisms · 2023Review
- Proximity Labeling Facilitates Defining the Proteome Neighborhood of Photosystem II Oxygen Evolution Complex in a Model Cyanobacterium.Molecular & cellular proteomics : MCP · 2022Article
- Advances in the Understanding of the Lifecycle of Photosystem II.Microorganisms · 2022Review
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
Cyanobacteria possess unique intracellular organization. Many proteomic studies have examined different features of cyanobacteria to learn about the intracellular structures and their respective functions. While these studies have made great progress in understanding cyanobacterial physiology, the conventional fractionation methods used to purify cellular structures have limitations; specifically, certain regions of cells cannot be purified with existing fractionation methods. Proximity-based proteomics techniques were developed to overcome the limitations of biochemical fractionation for proteomics. Proximity-based proteomics relies on spatiotemporal protein labeling followed by mass spectrometry of the labeled proteins to determine the proteome of the region of interest. We performed proximity-based proteomics in the cyanobacterium Synechococcus sp. PCC 7002 with the APEX2 enzyme, an engineered ascorbate peroxidase. We determined the proteome of the thylakoid lumen, a region of the cell that has remained challenging to study with existing methods, using a translational fusion between APEX2 and PsbU, a lumenal subunit of photosystem II. Our results demonstrate the power of APEX2 as a tool to study the cell biology of intracellular features and processes, including photosystem II assembly in cyanobacteria, with enhanced spatiotemporal resolution.
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