L protein, encoded by psbL, restores normal functioning of the primary quinone acceptor, QA, in isolated D1/D2/CP47/Cytb-559/I photosystem II reaction center core complex.
Plastoquinone-9 (PQ-9)-depleted PSII reaction center core complex, consisting of CP47/D1/D2/Cytb-559/I, was isolated from spinach PSII particles. PQ-9, lipids and several proteins were extracted from the original PSII particles and separated by several steps of chromatography to be reconstituted into the isolated complex. PQ-9 reconstituted in the complex with the help of thylakoid lipids (digalactosyldiglyceride) did not function as QA by itself. However, PQ-9 simultaneously reconstituted with L protein and the thylakoid lipids successfully functioned as QA in the complex. Other proteins of PSII origin, such as CP43, H, K, nuclear encoded 4.1 and 5.0 kDa proteins, are unable to restore the QA activity in the complex.
Graduate School of Human and Environmental Studies, Kyoto University, Japan.
K
K
Kitamura
S
S
Ozawa
T
T
Shiina
Y
Y
Toyoshima
D000818:Animals; D050356:Lipid Metabolism; D008055:Lipids / Q000302:isolation & purification; D045322:Photosynthetic Reaction Center Complex Proteins / Q000302:isolation & purification / Q000378:metabolism*; D045332:Photosystem II Protein Complex; D010971:Plastoquinone / Q000302:isolation & purification / Q000378:metabolism; D011809:Quinones / Q000378:metabolism; D018724:Spinacia oleracea / Q000502:physiology
D008055:Lipids; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D011809:Quinones; C075419:photosystem II, psbL subunit; D010971:Plastoquinone