The 33 kDa protein can be removed without affecting the association of the 23 and 17 kDa proteins with the luminal side of PS II of spinach

Biochemistry
Hui YuR David Britt

Abstract

An earlier study shows that a 30 min incubation of spinach PS II submembrane fragments at pH 6.3 in the presence of 10 microM HgCl(2) induces a 40% depletion of the 33 kDa protein without the apparent release of the 17 and 23 kDa proteins [Bernier, M., and Carpentier, R. (1995) FEBS Lett. 360, 251-254]. Here we report that the photosystem II 33 kDa extrinsic protein is fully removed by HgCl(2) added at micromolar and higher concentrations (0.25, 20, and 50 microM), with the 17 and 23 kDa extrinsic proteins and other intrinsic proteins remaining bound to the reaction center. The data presented here put in doubt the "regulatory cap" model of PS II, which follows the OEC-33 kDa-23 kDa-17 kDa binding order, as these results directly demonstrate that the 33 kDa protein can be removed without affecting the binding of the 23 and 17 kDa proteins to the intrinsic subunits of PS II. This suggests that each extrinsic protein may possess its own binding site on PS II. A possible mechanism for HgCl(2) upon the release of the 33 kDa protein is discussed.

References

Oct 16, 1992·Biochimica Et Biophysica Acta·R J Debus
Jan 9, 2003·Proceedings of the National Academy of Sciences of the United States of America·Nobuo Kamiya, Jian-Ren Shen
Apr 22, 2004·Biochimica Et Biophysica Acta·Idelisa Pujols-Ayala, Bridgette A Barry

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Citations

Jan 4, 2007·Photosynthesis Research·Johnna L RooseHimadri B Pakrasi
Feb 15, 2011·Journal of Photochemistry and Photobiology. B, Biology·Hana Popelkova, Charles F Yocum
Aug 2, 2011·Biochimica Et Biophysica Acta·Terry M BrickerJulian J Eaton-Rye
Aug 11, 2020·The Plant Journal : for Cell and Molecular Biology·John N FergusonErik H Murchie

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