- Integration of CiNii Books functions for fiscal year 2025 has completed
- Trial version of CiNii Research Knowledge Graph Search feature is available on CiNii Labs
- 【Updated on November 26, 2025】Regarding the recording of “Research Data” and “Evidence Data”
- Incorporated Jxiv preprints from JaLC and adding coverage from NDL Search
The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I
Bibliographic Information
- Published
- 2021-02
- Resource Type
- journal article
- Rights Information
-
- https://www.elsevier.com/tdm/userlicense/1.0/
- https://www.elsevier.com/legal/tdmrep-license
- http://creativecommons.org/licenses/by-nc-nd/4.0/
- DOI
-
- 10.1016/j.isci.2021.102059
- Publisher
- Elsevier BV
Search this article
Description
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.
Journal
-
- iScience
-
iScience 24 (2), 102059-, 2021-02
Elsevier BV
