Novel approach reveals localisation and assembly pathway of the PsbS and PsbW proteins into the photosystem II dimer. Thidholm, E., Lindström, V., Tissier, C., Robinson, C., P. Schröder, W., & Funk, C. FEBS Letters, 513(2-3):217–222, 2002. _eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2802%2902314-1![Novel approach reveals localisation and assembly pathway of the PsbS and PsbW proteins into the photosystem II dimer [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex A blue-native gel electrophoresis system was combined with an in organello import assay to specifically analyse the location and assembly of two nuclear-encoded photosystem II (PSII) subunits. With this method we were able to show that initially the low molecular mass PsbW protein is not associated with the monomeric form of PSII. Instead a proportion of newly imported PsbW is directly assembled in dimeric PSII supercomplexes with very fast kinetics; its negatively charged N-terminal domain is essential for this process. The chlorophyll-binding PsbS protein, which is involved in energy dissipation, is first detected in the monomeric PSII subcomplexes, and only at later time points in the dimeric form of PSII. It seems to be bound tighter to the PSII core complex than to light harvesting complex II. These data point to radically different assembly pathways for different PSII subunits.
@article{thidholm_novel_2002,
title = {Novel approach reveals localisation and assembly pathway of the {PsbS} and {PsbW} proteins into the photosystem {II} dimer},
volume = {513},
copyright = {FEBS Letters 513 (2002) 1873-3468 © 2015 Federation of European Biochemical Societies},
issn = {1873-3468},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1016/S0014-5793%2802%2902314-1},
doi = {10/c8cg4v},
abstract = {A blue-native gel electrophoresis system was combined with an in organello import assay to specifically analyse the location and assembly of two nuclear-encoded photosystem II (PSII) subunits. With this method we were able to show that initially the low molecular mass PsbW protein is not associated with the monomeric form of PSII. Instead a proportion of newly imported PsbW is directly assembled in dimeric PSII supercomplexes with very fast kinetics; its negatively charged N-terminal domain is essential for this process. The chlorophyll-binding PsbS protein, which is involved in energy dissipation, is first detected in the monomeric PSII subcomplexes, and only at later time points in the dimeric form of PSII. It seems to be bound tighter to the PSII core complex than to light harvesting complex II. These data point to radically different assembly pathways for different PSII subunits.},
language = {en},
number = {2-3},
urldate = {2021-10-19},
journal = {FEBS Letters},
author = {Thidholm, Ellinor and Lindström, Viktoria and Tissier, Christophe and Robinson, Colin and P. Schröder, Wolfgang and Funk, Christiane},
year = {2002},
note = {\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793\%2802\%2902314-1},
keywords = {5-bisphosphate carboxylase/oxygenase, Assembly, BN-PAGE, Blue-native polyacrylamide gel electrophoresis, Import, LHCII, PSI, PSII, PVDF, Photosystem II dimer, PsbS, PsbW, Rubisco, SDS, blue-native polyacrylamide gel electrophoresis, light harvesting complex II, n-dodecyl-β-D-maltoside, pPsbS, pPsbW, photosystem I and photosystem II, polyvinylidene difluoride, precursors of PsbW and PsbS, respectively, ribulose-1, sodium dodecyl sulphate, β-DM},
pages = {217--222},
}
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