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PLANT PHYSIOLOGY , Vol 115, Issue 4 1473-1480, Copyright © 1997 by American Society of Plant Biologists
Thermal Protection of the Oxygen-Evolving Machinery by PsbU, an Extrinsic Protein of Photosystem II, in Synechococcus species PCC 7002
Y. Nishiyama, D. A. Los, H. Hayashi and N. Murata
Department of Regulation Biology, National Institute for Basic Biology, Okazaki 444, Japan (Y.N., D.A.L., N.M.)
The evolution of oxygen is the reaction that is the most susceptible to
heat in photosynthesis. We showed previously that, in the cyanobacterium
Synechococcus sp. PCC 7002, some protein factors located on the thylakoid
membranes are involved in the stabilization of this reaction against
heat-induced inactivation, and we identified cytochrome c550 as one such
factor (Y. Nishiyama, H. Hayashi, T. Watanabe, N. Murata [1994] Plant
Physiol 105: 1313-1319). In the present study we purified another protein
that appears to be essential for the stabilization of the oxygen-evolving
machinery. The purified protein had an apparent molecular mass of 13 kD,
and the gene encoding the 13-kD protein was cloned from Synechococcus sp.
PCC 7002 and sequenced. The deduced amino acid sequence revealed that the
protein was homologous to PsbU, an extrinsic protein of the photosystem II
complex, which has been found in thermophilic species of cyanobacteria.
Western analysis showed that the level of PsbU in thylakoid membranes was
constant, regardless of the growth temperature. Our studies indicate that
PsbU, a constituent of the photosystem II complex, protects the
oxygen-evolving machinery against heat-induced inactivation.
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