Ask about this productRelated genes to: PEO1 antibody
- Gene:
- TWNK NIH gene
- Name:
- twinkle mtDNA helicase
- Previous symbol:
- IOSCA, C10orf2
- Synonyms:
- PEO, PEO1, TWINKLE, FLJ21832, TWINL
- Chromosome:
- 10q24.31
- Locus Type:
- gene with protein product
- Date approved:
- 2000-08-11
- Date modifiied:
- 2016-10-11
Related products to: PEO1 antibody
Related articles to: PEO1 antibody
- - Source: PubMed
Publication date: 2026/08/19
Yoshida ChiharuKubota AkatsukiKawamoto NorifumiTakahashi KensukeYano SatokaKomaki ShogoMaeda MeikoNaruse HiroyaMatsukawa TakashiHamada MasashiSatake WataruToda Tatsushi - - Source: PubMed
Publication date: 2026/08/19
Finsterer Josef - Replication of human mitochondrial DNA (mtDNA) is essential for the maintenance of oxidative phosphorylation and cellular energy homeostasis. Impairment of this process leads to mtDNA deletions, depletion, and point mutations that underlie a broad spectrum of mitochondrial diseases, as well as contributing to neurodegeneration, aging, and cancer. The core human mitochondrial replisome, composed of DNA polymerase γ (Polγ), the replicative helicase Twinkle, and the mitochondrial single-stranded DNA-binding protein (mtSSB), is the main complex responsible for replicating the mitochondrial genome through a highly coordinated yet still incompletely understood mechanism. Mutations in the nuclear genes encoding these proteins represent the most common cause of inherited disorders affecting mtDNA maintenance, underscoring the importance of understanding their coordinated molecular function. Recent advances in cryo-electron microscopy and single-molecule approaches have provided unprecedented insight into the structural organization and dynamic operation of the core components of the mitochondrial replisome. These complementary methods are establishing a quantitative mechanistic framework for understanding how the mitochondrial replisome initiates, progresses, and regulates the replication of the light and heavy strands of mtDNA. In the present review, we integrate recent structural and single-molecule findings to describe the mechanisms governing the activity of Polγ, Twinkle, and mtSSB at the mitochondrial replication fork, and discuss remaining challenges toward reconstructing a complete mechanistic model of human mtDNA replication. - Source: PubMed
Plaza-G A IsmaelMiguez-Amil SamuelHayes Allison MCiesielski Grzegorz LFernandez-Leiro RafaelIbarra Borja - Chronic progressive external ophthalmoplegia (CPEO) is a mitochondrial disease, with most sporadic cases caused by a single large mitochondrial DNA (mtDNA) deletion. We report the case of a 54-year-old woman with ptosis, external ophthalmoplegia, and proximal muscle weakness without any relevant family history. A muscle biopsy supported the diagnosis of sporadic CPEO. However, a muscle DNA analysis revealed multiple mitochondrial DNA (mtDNA) deletions. Whole-exome sequencing identified a heterozygous pathogenic TWNK variant [c.1121G>A (p.Arg374Gln)] absent in her parents, suggesting a de novo origin. Although TWNK pathogenic variants typically cause autosomal dominant CPEO, this case mimicked a sporadic form, thus highlighting the importance of a nuclear gene analysis in such cases. - Source: PubMed
Publication date: 2026/06/27
Yoshida ChiharuKubota AkatsukiKawamoto NorifumiTakahashi KensukeYano SatokaKomaki ShogoMaeda MeikoNaruse HiroyaMatsukawa TakashiHamada MasashiSatake WataruToda Tatsushi - Alternative splicing (AS) is prevalent in neuronal gene expression. However, its function in learning has not been systematically characterized. Here, by profiling pan-neuronal translatome changes during a learning paradigm, we show that AS remodels expression of neuronal genes with critical function in learning at the genome-wide scale. Intriguingly, AS operates on a functionally distinct gene set from those showing transcript abundance changes, serving as a separate regulatory layer in response to experience. Specifically, a neuronally enriched worm ortholog of a mitochondrial DNA helicase displays significant learning-associated AS changes, with both isoform types acting in a pair of sensory neurons to regulate learning with distinct functions. AS of modulates a cell-nonautonomous signal from neuronal mitochondria to peripheral tissues to regulate physiological states critical for learning. These results establish AS as a systematic regulator of learning and mechanistically reveal how AS shapes physiological states to facilitate learning. - Source: PubMed
Publication date: 2026/06/12
Chen MaotingWu MinKoterniak BinaGe MinghaiLiang JingtingCalarco JohnZhang Yun