Crucial role and conservation of the three [2Fe-2S] clusters in the human mitochondrial ribosome.

ABSTRACT: Mitochondria synthesize only a small set of their proteins on endogenous mitoribosomes. These particles differ in structure and composition from both their bacterial 70S ancestors and cytosolic 80S ribosomes. Recently published high resolution structures of the human mitoribosome revealed the presence of three [2Fe-2S] clusters in the small and large subunits. Each of these clusters is coordinated in a bridging fashion by cysteine residues from two different mitoribosomal proteins. Here, we investigated the cell biological and biochemical roles of all three iron-sulfur clusters in mitochondrial function and assembly. First, we found a requirement of both early and late factors of the mitochondrial iron-sulfur cluster assembly machinery for protein translation indicating that not only the m

SUBMITTER: Boß L 

PROVIDER: S-EPMC11791143 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature