Proximity-based proteomics reveals the thylakoid lumen proteome in the cyanobacterium Synechococcus sp. PCC 7002.
APEX2
Cyanobacteria
Photosynthesis
Photosystem II
Proximity-based proteomics
Thylakoid lumen
Journal
Photosynthesis research
ISSN: 1573-5079
Titre abrégé: Photosynth Res
Pays: Netherlands
ID NLM: 100954728
Informations de publication
Date de publication:
Feb 2021
Feb 2021
Historique:
received:
28
07
2020
accepted:
23
11
2020
pubmed:
7
12
2020
medline:
6
10
2021
entrez:
6
12
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 33280076
doi: 10.1007/s11120-020-00806-y
pii: 10.1007/s11120-020-00806-y
pmc: PMC7880944
doi:
Substances chimiques
Bacterial Proteins
0
Photosystem II Protein Complex
0
Proteome
0
Ascorbate Peroxidases
EC 1.11.1.11
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
177-195Subventions
Organisme : Biological and Environmental Research
ID : DE-SC0019306
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