TY - JOUR
T1 - Photosystem II complex in vivo is a monomer
AU - Takahashi, Takeshi
AU - Inoue-Kashino, Natsuko
AU - Ozawa, Shin Ichiro
AU - Takahashi, Yuichiro
AU - Kashino, Yashuhiro
AU - Satoh, Kazuhiko
PY - 2009/6/5
Y1 - 2009/6/5
N2 - Photosystem II (PS II) complexes are membrane protein complexes that are composed of >20 distinct subunit proteins. Similar to many other membrane protein complexes, two PS II complexes are believed to form a homo-dimer whose molecular mass is ∼650 kDa. Contrary to this well known concept, we propose that the functional form of PS II in vivo is a monomer, based on the following observations. Deprivation of lipids caused the conversion of PS II from a monomeric form to a dimeric form. Only a monomeric PS II Was detected in solubilized cyanobacterial and red algal thylakoids using blue-native polyacrylamide gel electrophoresis. Furthermore, energy transfer between PS II units, which was observed in the purified dimeric PS II, was not detected in vivo. Our proposal will lead to a re-evaluation of many crystallographic models of membrane protein complexes in terms of their oligomerization status.
AB - Photosystem II (PS II) complexes are membrane protein complexes that are composed of >20 distinct subunit proteins. Similar to many other membrane protein complexes, two PS II complexes are believed to form a homo-dimer whose molecular mass is ∼650 kDa. Contrary to this well known concept, we propose that the functional form of PS II in vivo is a monomer, based on the following observations. Deprivation of lipids caused the conversion of PS II from a monomeric form to a dimeric form. Only a monomeric PS II Was detected in solubilized cyanobacterial and red algal thylakoids using blue-native polyacrylamide gel electrophoresis. Furthermore, energy transfer between PS II units, which was observed in the purified dimeric PS II, was not detected in vivo. Our proposal will lead to a re-evaluation of many crystallographic models of membrane protein complexes in terms of their oligomerization status.
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U2 - 10.1074/jbc.M109.000372
DO - 10.1074/jbc.M109.000372
M3 - Article
C2 - 19351885
AN - SCOPUS:67650165736
SN - 0021-9258
VL - 284
SP - 15598
EP - 15606
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 23
ER -