title: Is the photosystem II complex a monomer or a dimer?
abstract: It is widely believed that the photosystem II (PSII) complex may function as a dimer in the thylakoid membrane. Here, we report experimental conversion from the monomeric PSII to the dimeric form by treatment with high concentrations of n-dodecyl-beta-D-maltopyranoside (DM). The content of the PSII monomer in a PsbTc deletion mutant was much higher than in the wild type when solubilized with low concentrations of DM. However, upon treatment with higher concentrations of DM, the PSII dimer was also recovered in the PsbTc deletion mutant. These results suggest that there are at least two distinct processes of dimerization: (i) PsbTc dependent and (ii) DM induced. We discuss the results with regard to the native assembly form(s) of PSII.
authors: Department of Life Sciences (Biology), Graduate School of Arts and Science, University of Tokyo, Meguro, Tokyo, Japan.
authors: Mai
authors: M
authors: Watanabe
authors: Masako
authors: M
authors: Iwai
authors: Rei
authors: R
authors: Narikawa
authors: Masahiko
authors: M
authors: Ikeuchi
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D000458:Cyanobacteria / Q000201:enzymology* / Q000235:genetics; D008320:Maltose / Q000031:analogs & derivatives / Q000494:pharmacology; D045332:Photosystem II Protein Complex / Q000235:genetics / Q000378:metabolism*; D055503:Protein Multimerization; D017384:Sequence Deletion; D020524:Thylakoids / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D045332:Photosystem II Protein Complex; C411362:dodecyl maltopyranoside; C093489:photosystem II, psbT subunit; D008320:Maltose