Ask about this productRelated genes to: MMS19 antibody
- Gene:
- MMS19 NIH gene
- Name:
- MMS19 homolog, cytosolic iron-sulfur assembly component
- Previous symbol:
- MMS19L
- Synonyms:
- MET18, hMMS19, CIAO4
- Chromosome:
- 10q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-12-21
- Date modifiied:
- 2018-05-17
Related products to: MMS19 antibody
Related articles to: MMS19 antibody
- Although emerging evidence revealed that molecular hydrogen (H) positively regulates numerous physiological responses, understanding the synthesis of H and its functions is a challenge for biology. - Source: PubMed
Publication date: 2026/04/16
Cheng PengfeiWang YueqiaoJiang KeCai ChenxuWang JunZhang YingyingLi LongnaHuang LiqinZeng YanPathier DidierCheng XuCui WeitiShen Wenbiao - - Source: PubMed
Publication date: 2026/03/06
Fu Yi-ChengLiu Le-PingZhou Yan-PingYang Ming-Hua - Cadmium (Cd) pollution is a global concern. Protists represent a prevalent yet understudied group in soil ecosystems, but our understanding of how protists interact with Cd remains limited. This study investigates the interaction between Cd and the soil amoeba Dictyostelium discoideum, focusing on its resistance, accumulation, and molecular mechanisms. We found that D. discoideum amoebae exhibit strong Cd resistance with an EC50 (half maximal effective concentration) of 899.2 mg/kg and demonstrates significant Cd enrichment capabilities, achieving concentrations up to 1094.70 ± 310.95 mg/kg in stalks and a bioconcentration factor (BCF) of 7.30. Transcriptomic analysis revealed enriched pathways related to DNA replication and identified key genes involved in metal transport, detoxification, and stress response, including abc4, abc16, mms19, gcsA, ucpB, and sodA. Notably, microRNA (miRNA) regulation was found to play a critical role in modulating the expression of these genes. Our findings provide novel insights into the Cd enrichment potential of D. discoideum amoebae and elucidate its mechanisms of heavy metal resistance, highlighting the regulatory role of miRNAs. This study not only advances our understanding of protist-Cd interactions but also opens new avenues for the bioremediation of heavy metal-contaminated soils, where soil amoebae could serve as an effective agent due to their high bioaccumulation factor and rapid growth cycle. - Source: PubMed
Publication date: 2025/01/27
Zhao YuanchenZhang LinWang ZiheWu ChenyuanLiu FeiShu Longfei - Cigarette smoke (CS) has detrimental effects on placental growth and embryo development, but the underlying mechanisms remain unclear. This study aims to investigate the impact of CS on trophoblast cell proliferation and regulated cell death (RCD) by examining its interference with iron-sulfur cluster (ISC) proteins and the CIA pathway. Exposure to CS disrupted the cytosolic ISC assembly (CIA) pathway, downregulated ISC proteins, and decreased ISC maturation in the placenta of rats exposed to passive smoking. Studies using HTR-8/Sneo cells demonstrated that cigarette smoke extract (CSE) inhibits trophoblast proliferation, activates autophagy, and induces apoptosis by impairing the CIA pathway and ISC proteins. Molecular docking analysis revealed that nicotine and nicotyrine bind to and promote the autophagic-dependent degradation of MMS19, a key component of the CIA complex. MMS19 KD led to the autophagic degradation of several ISC proteins involved in DNA damage repair and mitochondrial respiratory function, thereby inhibiting cell proliferation. Additionally, MMS19 deficiency resulted in mitochondrial fragmentation, ROS accumulation, and the induction of autosis and apoptosis. Transcriptome analysis indicated that dysregulation of the SMAD pathway mediates mitochondrial damage induced by MMS19 KD. Analysis of placental tissues from maternal smokers further confirmed the disruption of ISC proteins and the SMAD pathway. This study suggests that disruption of the CIA pathway and ISC proteins contributes to placental maldevelopment induced by CS. Targeting the MMS19-SMAD pathway may offer a potential strategy to mitigate adverse pregnancy outcomes caused by CS. - Source: PubMed
Publication date: 2025/01/16
Zhou PeiJin FengYao ShenshenSun BenSun NiGuan HongboLiu Xiaomei - FANCJ/BRIP1, initially identified as DOG-1 (Deletions Of G-rich DNA) in Caenorhabditis elegans, plays a critical role in genome integrity by facilitating DNA interstrand cross-link repair and resolving G-quadruplex structures. Its function is tightly linked to a conserved [4Fe-4S] cluster-binding motif, mutations of which contribute to Fanconi anemia and various cancers. This study investigates the critical role of the iron-sulfur (Fe-S) cluster in DOG-1 and its relationship with the cytosolic iron-sulfur protein assembly targeting complex (CTC). We found that a DOG-1 mutant, expected to be defective in Fe-S cluster binding, is primarily localized in the cytoplasm, leading to heightened DNA damage sensitivity and G-rich DNA deletions. We further discovered that the deletion of mms-19, a nonessential CTC component, also resulted in DOG-1 sequestered in cytoplasm and increased DNA damage sensitivity. Additionally, we identified that CIAO-1 and CIAO-2B are vital for DOG-1's stability and repair functions but unlike MMS-19 have essential roles in C. elegans. These findings confirm the CTC and Fe-S cluster as key elements in regulating DOG-1, crucial for genome integrity. Additionally, this study advances our understanding of the CTC's role in Fe-S protein regulation and development in C. elegans, offering a model to study its impact on multicellular organism development. - Source: PubMed
Li XiaoPerdomo Ivette Maria MenendezRodrigues Alves Barbosa VictoriaDiao CatherineTarailo-Graovac Maja