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Plant and Cell Physiology Advance Access originally published online on October 28, 2007
Plant and Cell Physiology 2007 48(12):1758-1763; doi:10.1093/pcp/pcm148
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© The Author 2007. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved.
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and the Japanese Society of Plant Physiologists are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

Absence of the PsbZ Subunit Prevents Association of PsbK and Ycf12 with the PSII Complex in the Thermophilic Cyanobacterium Thermosynechococcus elongatus BP-1

Masako Iwai1,2,*, Takehiro Suzuki3, Naoshi Dohmae3, Yasunori Inoue1,2 and Masahiko Ikeuchi4

1 Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Yamazaki 2641, Noda, Chiba, 278-8510 Japan
2 Tissue Engineering Research Center, Research Institute of Biological Science, Tokyo University of Science, Yamazaki 2641, Noda, Chiba, 278-8510 Japan
3 Biomolecular Characterization Team, Advanced Development and Supporting Center, The Institute of Physical and Chemical Research (RIKEN), Hirosawa 2-1, Wako, Saitama, 351-0198 Japan and
4 Department of Life Sciences (Biology), University of Tokyo, Komaba 3-8-1, Meguro, Tokyo, 153-8902 Japan

*Corresponding author: E-mail, miwai{at}rs.noda.tus.ac.jp; Fax, +81-4-7123-9767.


  Abstract

PsbZ (Ycf9) is a membrane protein of PSII complexes and is highly conserved from cyanobacteria to plants. We deleted the psbZ gene in the thermophilic cyanobacterium, Thermosynechococcus elongatus. The mutant cells showed photoautotrophic growth indistinguishable from that of the wild type under low and standard light conditions, while they showed even better growth than the wild type under high light. The mutant accumulated less carotenoids and more phycobiliproteins than the wild type under high light, suggestive of tolerance to photoinhibition. The mutant cells evolved oxygen at a rate comparable with the wild type, while the PSII complex isolated from the mutant retained much lower activity than the wild type. N-terminal sequencing revealed that Ycf12 and PsbK proteins were almost lost in the PSII complex. These results indicate that PsbZ is involved in functional integrity of the PSII complex by stabilizing PsbK and Ycf12. We suggest that Ycf12 is an unidentified membrane-spanning polypeptide that is placed near PsbZ and PsbK in the crystal structure of PSII.

Keywords: PSII - PsbK - PsbZ - Thermosynechococcus elongatus - Ycf9 - Ycf12

Abbreviations: 2,6-DCBQ, 2,6-dichlorobenzoquinone; β-DM, n-dodecyl-β-D-maltoside; LHCII, light-harvesting complex II; µE, µmol photons.

(Received August 27, 2007; Accepted October 20, 2007)
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