Plant and Cell Physiology, 2003, Vol. 44, No. 8 820-827
© 2003 Oxford University Press
Comparison of Binding and Functional Properties of Two Extrinsic Components, Cyt c550 and a 12 kDa Protein, in Cyanobacterial PSII with Those in Red Algal PSII
1 Department of Biology, Tokyo University of Science, Kagurazaka 1-3, Shinjuku-ku, Tokyo, 162-8601 Japan
2 Tissue Engineering Research Center, Tokyo University of Science, Yamazaki, Noda, Chiba 278-8510 Japan
3 RIKEN Harima Institute, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan; PRESTO, Japan Science and Technology Corporation (JST).
Cyt c550 and 12 kDa protein are two extrinsic proteins of photosystem II (PSII) found in cyanobacteria and some eukaryotic algae. The binding patterns of these two extrinsic proteins are different between cyanobacterial (Thermosynechococcus vulcanus) and red algal (Cyanidium caldarium) PSIIs [Shen and Inoue (1993) Biochemistry 32: 1825; Enami et al. (1998) Biochemistry 39: 2787]. In order to elucidate the possible causes responsible for these differences, we first cloned the psbV gene encoding Cyt c550 from a red alga, Cyanidium caldarium, which was compared with the homologous sequences from other organisms. Cross-reconstitution experiments were then performed with different combinations of the extrinsic proteins and the cyanobacterial or red algal PSII. (1) Both the cyanobacterial and red algal Cyt c550 bound directly to the cyanobacterial PSII, whereas none of them bound directly to the red algal PSII, indicating that direct binding of Cyt c550 to PSII principally depends on the structure of PSII intrinsic proteins but not that of Cyt c550 itself. (2) Cyt c550 was functionally exchangeable between the red algal and the cyanobacterial PSII, and the red algal 12 kDa protein functionally bound to the cyanobacterial PSII, whereas the cyanobacterial 12 kDa protein did not bind to the red algal PSII. (3) The antibody against the cyanobacterial or red algal 12 kDa protein reacted with its original one but not with the homologous protein from the other organism, whereas the antibody against the red algal Cyt c550 reacted with both cyanobacterial and red algal Cyt c550. These results imply that the structure and function of Cyt c550 have been largely conserved, whereas those of the 12 kDa protein have been changed, in the two organisms studied here.
4 Corresponding author: E-mail, enami{at}rs.noda.tus.ac.jp; Fax, +81-4-7124-2150.
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