Journal
BIOCHEMICAL JOURNAL
Volume 474, Issue -, Pages 2145-2158Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BCJ20170256
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Funding
- Wellcome Trust [096919/Z/11/Z]
- Biotechnology and Biological Sciences Research Council [BB/F011520/1]
- BBSRC [BB/F011520/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F011520/1] Funding Source: researchfish
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Accurate assembly and maturation of human mitochondrial ribosomes is essential for synthesis of the 13 polypeptides encoded by the mitochondrial genome. This process requires the correct integration of 80 proteins, 1 mt (mitochondrial)-tRNA and 2 mt-rRNA species, the latter being post-transcriptionally modified at many sites. Here, we report that human ribosome-binding factor A (RBFA) is a mitochondrial RNA-binding protein that exerts crucial roles in mitoribosome biogenesis. Unlike its bacterial orthologue, RBFA associates mainly with helices 44 and 45 of the 12S rRNA in the mitoribosomal small subunit to promote dimethylation of two highly conserved consecutive adenines. Characterization of RBFA-depleted cells indicates that this dimethylation is not a prerequisite for assembly of the small ribosomal subunit. However, the RBFA-facilitated modification is necessary for completing mt-rRNA maturation and regulating association of the small and large subunits to form a functional monosome implicating RBFA in the quality control of mitoribosome formation.
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