The Arabidopsis FRIENDLY (FMT) protein interacts with NAC and determines where nuclear-encoded mitochondrial proteins are translated

ABSTRACT: Mitochondria are not only the powerhouses of the cell. They are also dynamic signaling hubs, playing a key role in cellular metabolism and adaptation. Proper mitochondrial function depends largely on the import of proteins encoded by the nucleus. Using RNA immunoprecipitation and proximity labeling (TurboID), we show that Arabidopsis thaliana FRIENDLY (FMT) protein specifically recognizes the mRNAs of several organellar-destined proteins, mostly mitochondrial, and is in close proximity to these proteins during their translation. Remarkably, when FMT is absent, its target mRNAs lose their correct cellular localization. Our TurboID approach also confirms the interaction between FMT and the Nascent polypeptide Associated Complex (NAC), a ribosome-associated platform involved in the maturation and sorting of nascent peptides. Taken together, these results suggest that FMT, through its interaction with NAC and the ribosome, is involved in the spatial regulation of translation in the cell. FMT itself is under tight cellular control. It is rapidly degraded under stress but is overproduced in specific conditions, such as germination, impacting mitochondrial activity. Since mitochondria act as signaling hubs, this regulation of FMT could help the cell to quickly adapt to changing environments.

INSTRUMENT(S):

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Seedling

SUBMITTER: Johana Chicher  

LAB HEAD: Anne-Marie Duchêne

PROVIDER: PXD061930 | Pride | 2026-03-05

REPOSITORIES: Pride