English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse
  1. View item / 
  2. Item Summary

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

Isolation of a novel heterodimeric PSII complex via strep-tagged PsbO

MPS-Authors
/persons/resource/persons192975

Meier-Credo,  Jakob       
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137770

Langer,  Julian David       
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;
Proteomics, Max Planck Institute for Brain Research, Frankfurt am Main, Germany;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Lambertz, J., Meier-Credo, J., Kucher, S., Bordignon, E., Langer, J. D., & Nowaczyk, M. M. (2023). Isolation of a novel heterodimeric PSII complex via strep-tagged PsbO. Biochimica et Biophysica Acta, Bioenergetics, 1864(2): 148953. doi:10.1016/j.bbabio.2022.148953.


Cite as: https://hdl.handle.net/21.11116/0000-000C-15F7-6
Abstract
The multi-subunit membrane protein complex photosystem II (PSII) catalyzes the light-driven oxidation of water and with this the initial step of photosynthetic electron transport in plants, algae, and cyanobacteria. Its biogenesis is coordinated by a network of auxiliary proteins that facilitate the stepwise assembly of individual subunits and cofactors, forming various intermediate complexes until fully functional mature PSII is present at the end of the process. In the current study, we purified PSII complexes from a mutant line of the thermophilic cyanobacterium Thermosynechococcus vestitus BP-1 in which the extrinsic subunit PsbO, characteristic for active PSII, was fused with an N-terminal Twin-Strep-tag. Three distinct PSII complexes were separated by ion-exchange chromatography after the initial affinity purification. Two complexes differ in their oligomeric state (monomeric and dimeric) but share the typical subunit composition of mature PSII. They are characterized by the very high oxygen evolving activity of approx. 6000 μmol O2·(mg Chl·h)−1. Analysis of the third (heterodimeric) PSII complex revealed lower oxygen evolving activity of approx. 3000 μmol O2·(mg Chl·h)−1 and a manganese content of 2.7 (±0.2) per reaction center compared to 3.7 (±0.2) of fully active PSII. Mass spectrometry and time-resolved fluorescence spectroscopy further indicated that PsbO is partially replaced by Psb27 in this PSII fraction, thus implying a role of this complex in PSII repair.