The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I. / Trinh, Mai Duy Luu; Miyazaki, Daichi; Ono, Sumire; Nomata, Jiro; Kono, Masaru; Mino, Hiroyuki; Niwa, Tatsuya; Okegawa, Yuki; Motohashi, Ken; Taguchi, Hideki; Hisabori, Toru; Masuda, Shinji.

In: iScience, Vol. 24, 102059, 2021.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Trinh, MDL, Miyazaki, D, Ono, S, Nomata, J, Kono, M, Mino, H, Niwa, T, Okegawa, Y, Motohashi, K, Taguchi, H, Hisabori, T & Masuda, S 2021, 'The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I', iScience, vol. 24, 102059. https://doi.org/10.1016/j.isci.2021.102059

APA

Trinh, M. D. L., Miyazaki, D., Ono, S., Nomata, J., Kono, M., Mino, H., Niwa, T., Okegawa, Y., Motohashi, K., Taguchi, H., Hisabori, T., & Masuda, S. (2021). The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I. iScience, 24, [102059]. https://doi.org/10.1016/j.isci.2021.102059

Vancouver

Trinh MDL, Miyazaki D, Ono S, Nomata J, Kono M, Mino H et al. The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I. iScience. 2021;24. 102059. https://doi.org/10.1016/j.isci.2021.102059

Author

Trinh, Mai Duy Luu ; Miyazaki, Daichi ; Ono, Sumire ; Nomata, Jiro ; Kono, Masaru ; Mino, Hiroyuki ; Niwa, Tatsuya ; Okegawa, Yuki ; Motohashi, Ken ; Taguchi, Hideki ; Hisabori, Toru ; Masuda, Shinji. / The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I. In: iScience. 2021 ; Vol. 24.

Bibtex

@article{96ff4cd3b75742a8859f60e62b75359c,
title = "The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I",
abstract = "In natural habitats, plants have developed sophisticated regulatory mechanisms to optimize the photosynthetic electron transfer rate at the maximum efficiency and cope with the changing environments. Maintaining proper P700 oxidation at photosystem I (PSI) is the common denominator for most regulatory processes of photosynthetic electron transfers. However, the molecular complexes and cofactors involved in these processes and their function(s) have not been fully clarified. Here, we identified a redox-active chloroplast protein, the triplet-cysteine repeat protein (TCR). TCR shared similar expression profiles with known photosynthetic regulators and contained two triplet-cysteine motifs (CxxxCxxxC). Biochemical analysis indicated that TCR localizes in chloroplasts and has a [3Fe-4S] cluster. Loss of TCR limited the electron sink downstream of PSI during dark-to-light transition. Arabidopsis pgr5-tcr double mutant reduced growth significantly and showed unusual oxidation and reduction of plastoquinone pool. These results indicated that TCR is involved in electron flow(s) downstream of PSI, contributing to P700 oxidation.",
keywords = "Faculty of Science, P700 oxidation, Iron-Sulfur Proteins, Photosynthesis, photosystem I",
author = "Trinh, {Mai Duy Luu} and Daichi Miyazaki and Sumire Ono and Jiro Nomata and Masaru Kono and Hiroyuki Mino and Tatsuya Niwa and Yuki Okegawa and Ken Motohashi and Hideki Taguchi and Toru Hisabori and Shinji Masuda",
year = "2021",
doi = "10.1016/j.isci.2021.102059",
language = "English",
volume = "24",
journal = "iScience",
issn = "2589-0042",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I

AU - Trinh, Mai Duy Luu

AU - Miyazaki, Daichi

AU - Ono, Sumire

AU - Nomata, Jiro

AU - Kono, Masaru

AU - Mino, Hiroyuki

AU - Niwa, Tatsuya

AU - Okegawa, Yuki

AU - Motohashi, Ken

AU - Taguchi, Hideki

AU - Hisabori, Toru

AU - Masuda, Shinji

PY - 2021

Y1 - 2021

N2 - In natural habitats, plants have developed sophisticated regulatory mechanisms to optimize the photosynthetic electron transfer rate at the maximum efficiency and cope with the changing environments. Maintaining proper P700 oxidation at photosystem I (PSI) is the common denominator for most regulatory processes of photosynthetic electron transfers. However, the molecular complexes and cofactors involved in these processes and their function(s) have not been fully clarified. Here, we identified a redox-active chloroplast protein, the triplet-cysteine repeat protein (TCR). TCR shared similar expression profiles with known photosynthetic regulators and contained two triplet-cysteine motifs (CxxxCxxxC). Biochemical analysis indicated that TCR localizes in chloroplasts and has a [3Fe-4S] cluster. Loss of TCR limited the electron sink downstream of PSI during dark-to-light transition. Arabidopsis pgr5-tcr double mutant reduced growth significantly and showed unusual oxidation and reduction of plastoquinone pool. These results indicated that TCR is involved in electron flow(s) downstream of PSI, contributing to P700 oxidation.

AB - In natural habitats, plants have developed sophisticated regulatory mechanisms to optimize the photosynthetic electron transfer rate at the maximum efficiency and cope with the changing environments. Maintaining proper P700 oxidation at photosystem I (PSI) is the common denominator for most regulatory processes of photosynthetic electron transfers. However, the molecular complexes and cofactors involved in these processes and their function(s) have not been fully clarified. Here, we identified a redox-active chloroplast protein, the triplet-cysteine repeat protein (TCR). TCR shared similar expression profiles with known photosynthetic regulators and contained two triplet-cysteine motifs (CxxxCxxxC). Biochemical analysis indicated that TCR localizes in chloroplasts and has a [3Fe-4S] cluster. Loss of TCR limited the electron sink downstream of PSI during dark-to-light transition. Arabidopsis pgr5-tcr double mutant reduced growth significantly and showed unusual oxidation and reduction of plastoquinone pool. These results indicated that TCR is involved in electron flow(s) downstream of PSI, contributing to P700 oxidation.

KW - Faculty of Science

KW - P700 oxidation

KW - Iron-Sulfur Proteins

KW - Photosynthesis

KW - photosystem I

U2 - 10.1016/j.isci.2021.102059

DO - 10.1016/j.isci.2021.102059

M3 - Journal article

C2 - 33554065

VL - 24

JO - iScience

JF - iScience

SN - 2589-0042

M1 - 102059

ER -

ID: 311339160