TY - JOUR
T1 - Functional role of Lys residues of Psb31 in electrostatic interactions with diatom photosystem II
AU - Nagao, Ryo
AU - Suzuki, Takehiro
AU - Dohmae, Naoshi
AU - Shen, Jian Ren
AU - Tomo, Tatsuya
N1 - Funding Information:
This study was supported by Grants-in-Aid for Scientific Research from JSPS (26840091 to RN and 17K07453 and 26220801 to TT).
Publisher Copyright:
© 2017 Federation of European Biochemical Societies
PY - 2017/10
Y1 - 2017/10
N2 - 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.
AB - 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.
KW - Chaetoceros gracilis
KW - Psb31
KW - diatom
KW - electrostatic interaction
KW - photosystem II
KW - site-directed mutagenesis
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U2 - 10.1002/1873-3468.12830
DO - 10.1002/1873-3468.12830
M3 - Article
C2 - 28862739
AN - SCOPUS:85030027718
SN - 0014-5793
VL - 591
SP - 3259
EP - 3264
JO - FEBS Letters
JF - FEBS Letters
IS - 20
ER -