Ask about this productRelated genes to: MTFMT antibody
- Gene:
- MTFMT NIH gene
- Name:
- mitochondrial methionyl-tRNA formyltransferase
- Previous symbol:
- -
- Synonyms:
- FMT1
- Chromosome:
- 15q22.31
- Locus Type:
- gene with protein product
- Date approved:
- 2005-07-19
- Date modifiied:
- 2016-01-15
Related products to: MTFMT antibody
Related articles to: MTFMT antibody
- In long-lived neurons, precise control of mitochondrial gene expression is critical for maintaining bioenergetic capacity and preventing dysfunction linked to neurodegeneration. This control is executed by nuclear-encoded mitochondrial central dogma (NEM-CD) genes, yet their tissue-specific regulation, particularly in large mammalian brains, remains poorly defined. We conducted a comparative transcriptomic analysis of 214 NEM-CD genes across four buffalo tissues (brain/cerebellum, heart, kidney, and ovary) to elucidate organ-specific regulatory strategies. RNA sequencing and differential expression analysis revealed a definitive quantitative hierarchy (kidney > heart > brain > ovary), with tissue identity explaining 46.36% of intra-species transcriptomic variance (PC1). While the heart and kidney upregulated structural oxidative phosphorylation (OXPHOS) and translational machinery to meet high-throughput demands, the brain uniquely enriched genes governing transcriptional elongation (e.g., TEFM), RNA surveillance (e.g., PNPT1), and DNA repair (OGG1, POLG). Crucially, these findings were anchored by targeted LC-MS/MS proteomic screening, identifying brain-exclusive mitochondrial specialists such as SFXN3 and SLC25A14 (UCP5). Intra-species analysis revealed that the buffalo neuronal program participates in a robust body-wide regulatory plan (systemic coherence; median ρ = 0.8027), a synchronized architecture also observed in humans (median ρ = 0.9264). Subsequent cross-species compression identified a core set of highly conserved mitochondrial regulatory genes (e.g., ANGEL2, AARS2, RECQL4, MTFMT) that maintain strict evolutionary stability between humans and buffalo. Collectively, this study identifies a conserved "Precision-over-Throughput" neuroprotective strategy in mammalian brains, prioritizing transcriptional fidelity and genome maintenance over biogenic volume. This shared regulatory framework provides a stable comparative foundation for understanding mitochondrial dysregulation in both humans and large farm animals, offering a high-fidelity roadmap for neurodegenerative research. - Source: PubMed
Publication date: 2026/08/17
Sadeesh E MLahamge Madhuri SAmpadi A NKumari SwetaMohiddin Roshan
- Source: PubMed
- Boar sperm quality serves as an important indicator of reproductive efficiency, playing a direct role in enhancing the output of livestock production. It has been demonstrated that mitochondrial protein translation is present in sperm and plays a crucial role in regulating sperm motility, capacitation and in vitro fertilization rate. The present study aimed to determine whether methionine supplementation enhances mitochondrial translation in boar sperm, thereby improving sperm quality. The results showed a significant elevation in the abundance of mitochondrial methionyl-tRNA formyltransferase (MTFMT), a crucial enzyme for mitochondrial protein translation, and mitochondrial DNA-encoded cytochrome c oxidase subunit 1 (COX1) in boar sperm exhibiting high motility. Both amino acids and methionine supplementation significantly enhanced boar sperm motility during storage. Moreover, methionine supplementation mitigates the loss of acrosomal integrity, enhances the expression of COX1, and boosts mitochondrial activity. Furthermore, the positive impact of methionine was negated in the presence of the mitochondrial translation inhibitor chloramphenicol. Together, these findings suggest that boar sperm may utilize methionine as a protein translation substrate to enhance sperm motility by stimulating mitochondrial protein translation. The supplementation of methionine may enhance the quality of boar sperm, thereby providing guidance for the optimization of diluent formulations for liquid storage and the identification of physiological regulators that regulate sperm motility. - Source: PubMed
Publication date: 2024/07/31
Tan MeilingZhao YutingRen LiLi ChenxuanCai JiangxueHe Bin - Mitochondrial N-formylpeptides are released from damaged or dead cells to the extracellular spaces and cause inflammatory responses. The role of mitochondrial N-formylpeptides in aseptic systemic inflammatory response syndromes induced by trauma or cardiac surgery has been well investigated. However, there are no reports regarding the role of mitochondrial N-formylpeptides in cancer. In this study, we investigated the role of tumor cell-derived mitochondrial N-formylpeptides in anti-tumor immunity using knockout murine tumor cells of mitochondrial methionyl-tRNA formyltransferase (MTFMT), which catalyze N-formylation of mitochondrial DNA-encoded proteins. There was no apparent difference among the wild-type and MTFMT-knockout clones of E.G7-OVA cells with respect to morphology, mitochondrial dynamics, glycolysis and oxidative phosphorylation, oxygen consumption rate, or in vitro cell growth. In contrast, in vivo tumor growth of MTFMT-knockout cells was slower than that of wild-type cells. A reduced number of myeloid-derived suppressor cells and an increase of cytotoxic T-lymphocytes in the tumor tissues were observed in the MTFMT-knockout tumors. These results suggested that tumor cell-derived mitochondrial N-formylpeptides had a negative role in the host anti-tumor immunity through modification of the tumor microenvironment. - Source: PubMed
Publication date: 2024/07/31
Waki KayokoOzawa MiyakoOhta KeisukeKomatsu NobukazuYamada Akira - Metabolic reprogramming is currently considered a hallmark of tumor and immune development. It is obviously of interest to identify metabolic enzymes that are associated with clinical prognosis in head and neck squamous cell carcinomas (HNSCC). - Source: PubMed
Publication date: 2024/04/16
Wang LuHe YeBai YijiangZhang ShuaiPang BoChen AnhaiWu Xuewen