Back to Search
Start Over
Absence of the PsbQ Protein Results in Destabilization of the PsbV Protein and Decreased Oxygen Evolution Activity in Cyanobacterial Photosystem II.
- Source :
-
Journal of Biological Chemistry . 7/28/2006, Vol. 281 Issue 30, p20834-20841. 8p. 2 Charts, 6 Graphs. - Publication Year :
- 2006
-
Abstract
- We have previously reported that cyanobacterial photosystem II (PS II) contains a protein homologous to PsbQ, the extrinsic 17-kDa protein found in higher plant and green algal PS II (Kashino, Y., Lauber, W. M., Carroll, J. A., Wang, Q., Whitmarsh, J., Satoh, K., and Pakrasi, H. B. (2002) Biochemistry 41, 8004°8012) and that it has regulatory role(s) on the water oxidation machinery (Thornton, L. E., Ohkawa, H., Roose, J. L., Kashino, Y., Keren, N., and Pakrasi, H. B. (2004) Plant Cell 16, 2164°2175). In this work, the localization and the function of PsbQ were assessed using the cyanobacterium Synechocystis sp. PCC 6803. From the predicted sequence, cyanobacterial PsbQ is expected to be a lipoprotein on the luminal side of the thylakoid membrane. Indeed, experiments in this work show that upon Triton X-114 fractionation of thylakoid membranes, PsbQ partitioned in the hydrophobic phase, and trypsin digestion revealed that PsbQ was highly exposed to the luminal space of thylakoid membranes. Detailed functional assays were conducted on the psbQ deletion mutant (ΔpsbQ) to analyze its water oxidation machinery. PS II complexes purified from ΔpsbQ mutant cells had impaired oxygen evolution activity and were remarkably sensitive to NH2OH, which indicates destabilization of the water oxidation machinery. Additionally, the cytochrome c550 (PsbV) protein partially dissociated from purified ΔpsbQ PS II complexes, suggesting that PsbQ contributes to the stability of PsbV in cyanobacterial PS II. Therefore, we conclude that the major function of PsbQ is to stabilize the PsbV protein, thereby contributing to the protection of the catalytic Mn4-Ca1-Clx cluster of the water oxidation machinery. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00219258
- Volume :
- 281
- Issue :
- 30
- Database :
- Academic Search Index
- Journal :
- Journal of Biological Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 21988066
- Full Text :
- https://doi.org/10.1074/jbc.M603188200