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ProteomicsNFU3 is an Fe-S cluster carrier protein that is implicated in photosystem I maturation (PsaA, PsaB, PsaC). Label free proteomic approach on nfu3-2 mutant allow the discovery of new potential client proteins
NFU3 is a Fe-S cluster carrier protein of Arabidopsis that allow the maturation of Fe-S cluster proteins in chloroplast. proteomic Label free experiment was carried out to monitored wich Fe-S cluster proteins are affected in nfu3-2 mutant background
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2021-09-09 | PXD020228 | Pride
Fe-s cluster photosynthesis 
UnknownFe-S cluster assembly pathways in bacteria.
Not available
S-EPMC2268281 | biostudies-literature
UnknownInterplay between oxygen and Fe-S cluster biogenesis: insights from the Suf pathway.
Not available
S-EPMC4172210 | biostudies-literature
UnknownLow-Light Anoxygenic Photosynthesis and Fe-S-Biogeochemistry in a Microbial Mat.
Not available
S-EPMC5934491 | biostudies-literature
UnknownFoliar Spraying with Compound Amino Acid-Iron Fertilizer Increases Leaf Fresh Weight, Photosynthesis, and Fe-S Cluster Gene Expression in Peach (Prunus persica (L.) Batsch).
Not available
S-EPMC7273464 | biostudies-literature
UnknownInteraction between Nbp35 and Cfd1 proteins of cytosolic Fe-S cluster assembly reveals a stable complex formation in Entamoeba histolytica.
Not available
S-EPMC4182839 | biostudies-literature
UnknownFe-S Protein Synthesis in Green Algae Mitochondria.
Not available
S-EPMC7911964 | biostudies-literature
UnknownTracking molecular evolution of photosynthesis by characterization of a major photosynthesis gene cluster from Heliobacillus mobilis.
Not available
S-EPMC24539 | biostudies-literature
UnknownInterplay between formation of photosynthetic complexes and expression of genes for iron-sulfur cluster assembly in Rhodobacter sphaeroides?
Not available
S-EPMC7728643 | biostudies-literature
TranscriptomicsAcclimation of oxygenic photosynthesis to iron starvation is controlled by the sRNA IsaR1 in cyanobacteria
Oxygenic photosynthesis contains multiple proteins that possess Fe2+ or Fe/S complexes as co-factors or prosthetic groups. Accordingly, its composition is heavily re-organized when iron becomes limiting as a nutrient factor, a situation that is frequently encountered in nature. However, the molecula...
ORGANISM(S): Synechocystis sp. PCC 6803 
2016-10-01 | GSE87496 | GEO
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