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Functional role of Lys residues of Psb31 in electrostatic interactions with diatom photosystem II
Author(s) -
Nagao Ryo,
Suzuki Takehiro,
Dohmae Naoshi,
Shen JianRen,
Tomo Tatsuya
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12830
Subject(s) - photosystem ii , mutant , biophysics , chemistry , protein subunit , wild type , photosystem i , biochemistry , biology , photosynthesis , gene
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 O 2 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 .