The chloroplastic NFU1 maturation factor sustains iron-sulfur cluster assembly in the dark in Chlamydomonas

Clicks: 1
ID: 319408
2026
Free PDF
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal

Ranked #476 of 502 articles by views in Plant physiology and biochemistry : PPB

Most read Least read

Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 502 in total.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
Abstract The sulfur mobilization (SUF) machinery is required for the synthesis of iron-sulfur (Fe-S) clusters and their insertion into client proteins in plastids. The final step relies on several Fe-S cluster transfer proteins, including NifU-like (NFU) proteins. In this study, we focused on the chloroplastic NFU1 from the green microalga Chlamydomonas reinhardtii. It possesses an N-terminal putative endonuclease domain that is absent in orthologs from angiosperms. Using a reverse genetic approach, we demonstrated that NFU1 serves as the major maturation factor for several [4Fe-4S]-cluster containing proteins involved in specialized pathways. This includes an atypical hybrid cluster protein, the pyruvate-ferredoxin oxidoreductase and an iron-iron hydrogenase operating in anoxia, as well as the dark-operative protochlorophyllide a oxidoreductase (DPOR) involved in chlorophyll synthesis in the dark. Based on the decreased abundance of chloroplast ribosomal proteins observed by proteomics in the nfu1 mutants, the lack of endonuclease activity of the N-terminal domain and the fact that NFU1 was previously reported as associated with chloroplast ribosomes, we propose that NFU1 contributes to the co-translational insertion of the [4Fe-4S] cluster(s) in the chloroplast-encoded DPOR subunits. The strong co-occurrence between genes encoding elongated NFU1 representatives and DPOR subunits in the green lineage supports this intertwined function and the importance of the N-terminal domain for NFU1 function.
Reference Key
openalex_W7167025754 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Jonathan Przybyla‐Toscano, Antoine Kairis, Agustina Terenzi, Anna Caccamo, Sébastien Pyr dit Ruys, Didier Vertommen, Nicolas Rouhier, Claire Remacle
Journal Plant physiology and biochemistry : PPB
Year 2026
DOI
10.1093/plphys/kiag466
URL
https://doi.org/10.1093/plphys/kiag466
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.