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Plant and Cell Physiology Advance Access first published online on October 28, 2007
This version published online on November 20, 2007
Plant and Cell Physiology, 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. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Absence of the PsbZ subunit prevents association of PsbK and Ycf12 with the photosystem II complex in the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1

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

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

Corresponding author: Dr. Masako Iwai, Tel. +81-4-7124-1501 ext.3422; FAX +81-4-7123-9767; E-mail miwai{at}rs.noda.tus.ac.jp


  Abstract

PsbZ (Ycf9) is a membrane protein of photosystem II (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 wild type under low and standard light conditions, while they showed even better growth than wild type under high light. The mutant accumulated less carotenoids and more phycobiliproteins than wild type under high light, suggestive of tolerance to photoinhibition. The mutant cells evolved oxygen at a rate comparable to wild type, while the PSII complex isolated from the mutant retained the activity much lower than 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: PsbZ - Ycf9 - photosystem II - PsbK - Ycf12 - Thermosynechococcus elongatus

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