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Dimeric and monomeric organization of photosystem II - Distribution of five distinct complexes in the different domains of the thylakoid membrane

Danielsson, Ravi LU ; Suorsa, M ; Paakkarinen, V ; Albertsson, Per-Åke LU ; Styring, S ; Aro, EM and Mamedov, F (2006) In Journal of Biological Chemistry 281(20). p.14241-14249
Abstract
The supramolecular organization of photosystem II (PSII) was characterized in distinct domains of the thylakoid membrane, the grana core, the grana margins, the stroma lamellae, and the so-called Y100 fraction. PSII supercomplexes, PSII core dimers, PSII core monomers, PSII core monomers lacking the CP43 subunit, and PSII reaction centers were resolved and quantified by blue native PAGE, SDS-PAGE for the second dimension, and immunoanalysis of the D1 protein. Dimeric PSII (PSII supercomplexes and PSII core dimers) dominate in the core part of the thylakoid granum, whereas the monomeric PSII prevails in the stroma lamellae. Considerable amounts of PSII monomers lacking the CP43 protein and PSII reaction centers (D1-D2-cytochrome b(559)... (More)
The supramolecular organization of photosystem II (PSII) was characterized in distinct domains of the thylakoid membrane, the grana core, the grana margins, the stroma lamellae, and the so-called Y100 fraction. PSII supercomplexes, PSII core dimers, PSII core monomers, PSII core monomers lacking the CP43 subunit, and PSII reaction centers were resolved and quantified by blue native PAGE, SDS-PAGE for the second dimension, and immunoanalysis of the D1 protein. Dimeric PSII (PSII supercomplexes and PSII core dimers) dominate in the core part of the thylakoid granum, whereas the monomeric PSII prevails in the stroma lamellae. Considerable amounts of PSII monomers lacking the CP43 protein and PSII reaction centers (D1-D2-cytochrome b(559) complex) were found in the stroma lamellae. Our quantitative picture of the supramolecular composition of PSII, which is totally different between different domains of the thylakoid membrane, is discussed with respect to the function of PSII in each fraction. Steady state electron transfer, flash-induced fluorescence decay, and EPR analysis revealed that nearly all of the dimeric forms represent oxygen-evolving PSII centers. PSII core monomers were heterogeneous, and a large fraction did not evolve oxygen. PSII monomers without the CP43 protein and PSII reaction centers showed no oxygen-evolving activity. (Less)
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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
281
issue
20
pages
14241 - 14249
publisher
ASBMB
external identifiers
  • wos:000237512300048
  • scopus:33744950039
ISSN
1083-351X
DOI
10.1074/jbc.M600634200
language
English
LU publication?
yes
id
3e409507-b85e-474d-a98c-967a0fb1a1d2 (old id 409497)
date added to LUP
2016-04-01 11:57:58
date last changed
2021-10-10 03:53:41
@article{3e409507-b85e-474d-a98c-967a0fb1a1d2,
  abstract     = {The supramolecular organization of photosystem II (PSII) was characterized in distinct domains of the thylakoid membrane, the grana core, the grana margins, the stroma lamellae, and the so-called Y100 fraction. PSII supercomplexes, PSII core dimers, PSII core monomers, PSII core monomers lacking the CP43 subunit, and PSII reaction centers were resolved and quantified by blue native PAGE, SDS-PAGE for the second dimension, and immunoanalysis of the D1 protein. Dimeric PSII (PSII supercomplexes and PSII core dimers) dominate in the core part of the thylakoid granum, whereas the monomeric PSII prevails in the stroma lamellae. Considerable amounts of PSII monomers lacking the CP43 protein and PSII reaction centers (D1-D2-cytochrome b(559) complex) were found in the stroma lamellae. Our quantitative picture of the supramolecular composition of PSII, which is totally different between different domains of the thylakoid membrane, is discussed with respect to the function of PSII in each fraction. Steady state electron transfer, flash-induced fluorescence decay, and EPR analysis revealed that nearly all of the dimeric forms represent oxygen-evolving PSII centers. PSII core monomers were heterogeneous, and a large fraction did not evolve oxygen. PSII monomers without the CP43 protein and PSII reaction centers showed no oxygen-evolving activity.},
  author       = {Danielsson, Ravi and Suorsa, M and Paakkarinen, V and Albertsson, Per-Åke and Styring, S and Aro, EM and Mamedov, F},
  issn         = {1083-351X},
  language     = {eng},
  number       = {20},
  pages        = {14241--14249},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Dimeric and monomeric organization of photosystem II - Distribution of five distinct complexes in the different domains of the thylakoid membrane},
  url          = {http://dx.doi.org/10.1074/jbc.M600634200},
  doi          = {10.1074/jbc.M600634200},
  volume       = {281},
  year         = {2006},
}