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Plant Physiol, December 1999, Vol. 121, pp. 1267-1272

The PsbY Protein Is Not Essential for Oxygenic Photosynthesis in the Cyanobacterium Synechocystis sp. PCC 68031

Metha Meetam, Nir Keren, Itzhak Ohad, and Himadri B. Pakrasi*

Department of Biology, Box 1137, Washington University, St. Louis, Missouri 63130 (M.M., H.B.P.); and Department of Biological Chemistry, The Hebrew University, Jerusalem 91904, Israel (N.K., I.O.)

A tetra-manganese cluster in the photosystem II (PSII) pigment-protein complex plays a critical role in the photosynthetic oxygen evolution process. PsbY, a small membrane-spanning polypeptide, has recently been suggested to provide a ligand for manganese in PSII (A.E. Gau, H.H. Thole, A. Sokolenko, L. Altschmied, R.G. Herrmann, E.K. Pistorius [1998] Mol Gen Genet 260: 56-68). We have constructed a mutant strain of the cyanobacterium Synechocystis sp. PCC 6803 with an inactivated psbY gene (sml0007). Southern-blot and polymerase chain reaction analysis showed that the mutant had completely segregated. However, the Delta psbY mutant cells grew normally under photoautotrophic conditions. Moreover, growth of the wild-type and mutant cells were similar under high-light photoinhibition conditions, as well as in media without any added manganese, calcium, or chloride, three required inorganic cofactors for the oxygen-evolving complex of PSII. Analysis of steady-state and flash-induced oxygen evolution, fluorescence induction, and decay kinetics, and thermoluminescence profiles demonstrated that the Delta psbY mutant cells have normal photosynthetic activities. We conclude that the PsbY protein in Synechocystis 6803 is not essential for oxygenic photosynthesis and does not provide an important binding site for manganese in the oxygen-evolving complex of PSII.

1 This work was supported by grants from the National Institutes of Health (to H.B.P.) and the International Human Frontier Science Program (to H.B.P. and I.O.). H.B.P.'s visit to Jerusalem was supported by a Lady Davis Visiting Professorship at the Hebrew University. M.M. was partially supported by a Development and Promotion of Science and Technology Talented Students scholarship from the government of Thailand and by a summer research fellowship from the Howard Hughes Medical Institute.

* Corresponding author; e-mail pakrasi{at}biology.wustl.edu; fax 314-935-6803.

© 1999 American Society of Plant Physiologists


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