期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1837, 期 9, 页码 1447-1453出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2013.12.012
关键词
Extrinsic protein; Higher plants; Oxygen-evolving complex; Photosystem II; PsbP
资金
- JST PRESTO
- JSPS [18770032]
- Grants-in-Aid for Scientific Research [26840091, 18770032, 24000018, 24107003, 23657099] Funding Source: KAKEN
The PsbP protein is an extrinsic subunit of photosystem II (PSII) that is essential for photoautotrophic growth in higher plants. Several crystal structures of PsbP have been reported, but the binding topology of PsbP in PSII has not yet been clarified. In this study, we report that the basic pocket of PsbP, which consists of conserved Arg48, Lys143, and Lys160, is important for the electrostatic interaction with the PSII complex. Our release-reconstitution experiment showed that the binding affinities of PsbP-R48A, -K143A, and -K160A mutated proteins to PSII were lower than that of PsbP-WT, and triple mutations of these residues greatly diminished the binding affinity to PSII. Even when maximum possible binding had occurred, the R48A, K143A, and K160A proteins showed a reduced ability to restore the rate of oxygen evolution at low chloride concentrations. Fourier transform infrared resonance (FTIR) difference spectroscopy results were consistent with the above finding, and suggested that these mutated proteins were not able to induce the normal conformational change around the Mn cluster during Si to S-2 transition. Finally, chemical cross-linking experiments suggested that the interaction between the N-terminus of PsbP with PsbE was inhibited by these mutations. These data suggest that the basic pocket of PsbP is important for proper association and interaction with PSII. This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: Keys to Produce Clean Energy. (C) 2013 Elsevier B.V. All rights reserved.
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