Identification of the basic amino acid residues on the PsbP protein involved in the electrostatic interaction with photosystem II

Taishi Nishimura, Chihiro Uno, Kunio Ido, Ryo Nagao, Takumi Noguchi, Fumihiko Sato, Kentaro Ifuku

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

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 S1 to S2 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.

Original languageEnglish
Pages (from-to)1447-1453
Number of pages7
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1837
Issue number9
DOIs
Publication statusPublished - 2014
Externally publishedYes

Fingerprint

Basic Amino Acids
Photosystem II Protein Complex
Coulomb interactions
Static Electricity
Proteins
Mutation
Photosynthesis
Fourier Analysis
Chlorides
Sustainable development
Spectrum Analysis
Fourier transforms
Crystal structure
Experiments
Topology
Association reactions
Spectroscopy
Oxygen
Infrared radiation
Growth

Keywords

  • Extrinsic protein
  • Higher plants
  • Oxygen-evolving complex
  • Photosystem II
  • PsbP

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology

Cite this

Identification of the basic amino acid residues on the PsbP protein involved in the electrostatic interaction with photosystem II. / Nishimura, Taishi; Uno, Chihiro; Ido, Kunio; Nagao, Ryo; Noguchi, Takumi; Sato, Fumihiko; Ifuku, Kentaro.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1837, No. 9, 2014, p. 1447-1453.

Research output: Contribution to journalArticle

Nishimura, Taishi ; Uno, Chihiro ; Ido, Kunio ; Nagao, Ryo ; Noguchi, Takumi ; Sato, Fumihiko ; Ifuku, Kentaro. / Identification of the basic amino acid residues on the PsbP protein involved in the electrostatic interaction with photosystem II. In: Biochimica et Biophysica Acta - Bioenergetics. 2014 ; Vol. 1837, No. 9. pp. 1447-1453.
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