Ask about this productRelated genes to: MTIF3 Blocking Peptide
- Gene:
- MTIF3 NIH gene
- Name:
- mitochondrial translational initiation factor 3
- Previous symbol:
- -
- Synonyms:
- IF-3mt, IF3(mt)
- Chromosome:
- 13q12.2
- Locus Type:
- gene with protein product
- Date approved:
- 2006-11-03
- Date modifiied:
- 2014-11-19
Related products to: MTIF3 Blocking Peptide
Related articles to: MTIF3 Blocking Peptide
- Advanced renal failure remains a major global health burden. Mitochondrial dysfunction is frequently observed during progressive kidney injury and chronic allograft dysfunction (CAD), but observational data cannot distinguish causal involvement from secondary consequences. We applied a multi-omic genetic prioritization framework to evaluate whether inherited variation affecting mitochondrial gene regulation is associated with a proxy phenotype for advanced renal failure and fibrotic allograft remodeling. - Source: PubMed
Publication date: 2026/03/27
Shen QinghuanDing RunminWen ZhiyuFeng DengyuanZhang JianjianLiu JiawenHan QianguangSun LiChen HaoFei ShuangXu ZhenHao RuijinlinTan Ruoyun - Mitochondrial translation is essential for cellular function, and its dysregulation is associated with mitochondrial disorders and cancer. However, the mechanisms by which human mitochondrial ribosomes initiate translation remain poorly understood, particularly because mitochondrial mRNAs generally lack the 5' untranslated regions that guide translation initiation in bacterial and cytoplasmic systems. Using real-time single-molecule fluorescence measurements, biochemical assays, and cryo-EM analysis, we show that human mitochondrial translation initiation occurs through two parallel pathways. In one pathway, leaderless mRNA first loads onto the 28S small subunit, followed by recruitment of the 39S large subunit to form the 55S initiation complex. In the second pathway, a preassembled 55S monosome directly loads onto leaderless mRNA. Both pathways require recruitment of mtIF2 and fMet-tRNA before mRNA binding. However, the monosome-loading pathway tolerates non-formylated Met-tRNA and is suppressed by mtIF3. Together, these findings define the heterogeneous pathways of human mitochondrial translation initiation on leaderless mRNAs. - Source: PubMed
Publication date: 2026/04/04
Shen ShuangjieXu YinghuaKober Daniel LWang Jinfan - Mitochondrial translation machinery exhibits similarities with the bacterial translation apparatus. Of the three bacterial translation initiation factors (IF1, IF2 and IF3), two (IF2 and IF3) have homologues in mitochondria (mtIF2 and mtIF3). A high conservation of decoding nucleotides in the ribosomal A-site suggests relevance of IF1-like proteins in mitochondria. The mitochondrial translation machineries have evolved with different solutions for the IF1 function. However, in , the identity of such a protein remains unknown. Here, based on sequence alignment with human mtIF2, we deduced that Rmd9p may contribute to an IF1-like function in . Our genetic analyses show that Rmd9p is required for mitochondrial translation. In addition, we show that a sequence from Rmd9p, pivotal for its mitochondrial function, when inserted into mtIF2, substitutes for both the IF2 and IF1 functions in an established model of . Interestingly, while the mutations at the critical residues in the Rmd9p peptide compromise the IF1 function, the mutant peptide is still able to support growth, suggesting that the structure (rather than the precise sequence) of the IF1-like insert domain in mitochondrial IF2 plays a major role in the recognition of the decoding nucleotides in the ribosomal A-site. - Source: PubMed
Singh JitendraSahu Amit KumarVarshney Umesh - Translation initiation, the first step of the translation cycle, involves initiation factors (mtIF) 2 and 3 in mitochondria. mtIF3 release from the ribosomal small subunit was believed to be a prerequisite for the recruitment of the initiator tRNA. Here we use cryogenic electron microscopy to characterize plant mitochondria pre-initiation complexes and to reveal how plant mtIF3 binds the initiator tRNA and facilitates its accommodation in the decoding center. - Source: PubMed
Publication date: 2025/12/30
Skaltsogiannis VasileiosSoufari HeddyGiegé Philippe - Since mitochondrial translation leads to the synthesis of the essential oxidative phosphorylation (OXPHOS) subunits, exhaustive and quantitative delineation of mitoribosome traversal is needed. Here, we developed a variety of high-resolution mitochondrial ribosome profiling derivatives and revealed the intricate regulation of mammalian mitochondrial translation. Harnessing a translation inhibitor, retapamulin, our approach assessed the stoichiometry and kinetics of mitochondrial translation flux, such as the number of mitoribosomes on a transcript, the elongation rate, and the initiation rate. We also surveyed the impacts of modifications at the anticodon stem loop in mitochondrial tRNAs (mt-tRNAs), including all possible modifications at the 34th position, in cells deleting the corresponding enzymes and derived from patients, as well as in mouse tissues. Moreover, a retapamulin-assisted derivative and mito-disome profiling revealed mitochondrial translation initiation factor (mtIF) 3-mediated translation initiation from internal open reading frames (ORFs) and programmed mitoribosome collision sites across the mitochondrial transcriptome. Our work provides a useful platform for investigating protein synthesis within the energy powerhouse of the cell. - Source: PubMed
Publication date: 2025/11/12
Wakigawa TaiseiMito MariAndo YushinYamashiro HarunaTomuro KotaroTani HarunaTomizawa KazuhitoChujo TakeshiNagao AsutekaSuzuki TakeoNureki OsamuWei Fan-YanShichino YuichiItoh YuzuruSuzuki TsutomuIwasaki Shintaro