Functional role of Lys residues of Psb31 in electrostatic interactions with diatom photosystem II

Ryo Nagao, Takehiro Suzuki, Naoshi Dohmae, Jian Ren Shen, Tatsuya Tomo

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

We recently revealed that positively charged amino acids of Psb31, an extrinsic subunit found in diatom photosystem II (PSII), are involved in electrostatic interactions with PSII intrinsic subunits. However, the molecular interactions of Psb31 with PSII remain unclear. Here, we report the functional contribution of Lys residues in the binding of Psb31 to PSII using site-directed mutants of Psb31. Each of the K33A, K39A, K54A, K56A, K57A, and K69A mutants exhibits decreased binding affinities to PSII concomitantly with decreases in the O2 evolution activity. Conversely, each of the K24A, K76A, K80A, and K117A mutants functionally binds to PSII in a manner similar to wild-type Psb31. These results provide evidence that some Lys residues of Psb31 are responsible for electrostatic interactions with PSII.

Original languageEnglish
Pages (from-to)3259-3264
Number of pages6
JournalFEBS Letters
Volume591
Issue number20
DOIs
Publication statusPublished - Oct 2017

Keywords

  • Chaetoceros gracilis
  • Psb31
  • diatom
  • electrostatic interaction
  • photosystem II
  • site-directed mutagenesis

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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