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
APA
Vancouver
Author
Bibtex
}
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