Ask about this productRelated genes to: NSMCE1 Blocking Peptide
- Gene:
- NSMCE1 NIH gene
- Name:
- NSE1 homolog, SMC5-SMC6 complex component
- Previous symbol:
- -
- Synonyms:
- NSE1
- Chromosome:
- 16p12.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-12
- Date modifiied:
- 2015-07-03
Related products to: NSMCE1 Blocking Peptide
Related articles to: NSMCE1 Blocking Peptide
- Smc5/6 is a protein complex with a ring structure that suppresses HBV transcription and proliferation. HBV counters this restriction by encoding the regulatory protein HBx, which targets Smc5/6 for proteasomal degradation. However, the molecular mechanism of HBV inhibition by Smc5/6 remains elusive. Here, we take advantage of a luciferase reporter gene in a cell-free expression system and measured the transcriptional activity using the purified Smc5/6 holo-complex, subcomplexes or individual subunits. Besides Smc5/6 holo-complex, NSMCE1/3 subcomplex is sufficient to inhibit transcription in vitro. NSMCE1/3 represses HBx expression at both the mRNA level and the protein level as revealed by the RT-PCR and a cycloheximide chase experiment, respectively. Overexpression of NSMCE1/3 causes degradation of HBx and this effect is blocked by a proteasome inhibitor but not by an inhibitor of the ubiquitin-activating enzyme E1. NSMCE1/3 interacts with the 20S proteasome but does not stimulate the ubiquitination of HBx, indicating that NSMCE1/3 leads to HBx degradation via a ubiquitin-independent proteasomal mechanism. Overexpression of NSMCE1/3 results in inhibition of HBV proliferation in hepatoma cell lines while knockdown of NSMCE3 leads to proliferation promotion. These new findings provide insights into the molecular mechanism of HBV inhibition by Smc5/6. - Source: PubMed
Publication date: 2026/03/11
He LiliShen HuanyuZhao AotingPan YuxuanMa JunOuyang Zhuqing - Chromosome organization undergoes substantial changes during S phase, as parental strands unzip at replication forks to create sister chromatids. Structural Maintenance of Chromosomes (SMC) complexes actively organize chromatin fibers in the wake of the replication fork during a normal S phase, but also in response to replicative stress, thereby influencing replication dynamics. The DNA fiber assay is a relatively simple and cheap technique that allows the study of replication dynamics by sequential incorporation of two nucleotide analogs, followed by DNA spreading and immunodetection of replicated tracks. Here, we present a step-by-step protocol to perform DNA fiber assays in human cell lines, providing a quantitative approach to analyze replication fork progression. As an example, we describe its application in wild-type and SMC5/6 mutant cells, treated or not with hydroxyurea to induce replicative stress. This method can be easily customized to other cell types, alternative strategies for SMC complex inactivation, or treatments that perturb DNA replication. In addition, by modifying culture conditions, this approach can be used to investigate not only fork rate but also fork reversal, fork restart, fork protection, and other aspects of global replication dynamics regulated by SMC activities. - Source: PubMed
Lorite Neus PSnehlata Colomina NeusTorres-Rosell JordiRodríguez-Acebes SaraMéndez Juan - Methotrexate (MTX) is the primary drug used in the treatment of pediatric acute lymphoblastic leukemia (ALL). However, some patients exhibit delayed clearance of high-dose (HD) MTX, which induces severe nephrotoxicity, mucositis, hepatotoxicity, and neurotoxicity. We sought to identify relevant variants associated with delayed clearance of HD-MTX in pediatric patients with ALL. - Source: PubMed
Publication date: 2024/11/14
Choi Jung YoonKwon HoshikKim HyeryHong Kyung TaekMa YoungeunKoh Kyung-NamYun SunminYoo Keon HeeSong Sang HoonIm Ho JoonKim Ju HanKang Hyoung Jin - The Smc5/6 complex is a highly conserved molecular machine involved in the maintenance of genome integrity. While its functions largely depend on restraining the fork remodeling activity of Mph1 in yeast, the presence of an analogous Smc5/6-FANCM regulation in humans remains unknown. We generated human cell lines harboring mutations in the NSE1 subunit of the Smc5/6 complex. Point mutations or truncations in the RING domain of NSE1 result in drastically reduced Smc5/6 protein levels, with differential contribution of the two zinc-coordinating centers in the RING. In addition, nse1-RING mutant cells display cell growth defects, reduced replication fork rates, and increased genomic instability. Notably, our findings uncover a synthetic sick interaction between Smc5/6 and FANCM and show that Smc5/6 controls fork progression and chromosome disjunction in a FANCM-independent manner. Overall, our study demonstrates that the NSE1 RING domain plays vital roles in Smc5/6 complex stability and fork progression through pathways that are not evolutionary conserved. - Source: PubMed
Publication date: 2024/06/07
Lorite Neus PApostolova SoniaGuasch-Vallés MartaPryer AaronUnzueta FernandoFreire RaimundoSolé-Soler RogerPedraza NeusDolcet XavierGarí EloiAgell NeusTaylor Elaine MColomina NeusTorres-Rosell Jordi - To reveal the core mechanism of berberine (BBR) in the treatment of diabetic retinopathy (DR), by using Four-dimensional independent data acquisition (4D-DIA) proteomics combined bioinformatics analysis with experimental validation. - Source: PubMed
Publication date: 2023/09/01
Na LiXu MinChen Ji-LinChen Guo-JiaoSun JieZhang QiangLi Jun-QiGuo Xi-LiangZuo Zhong-FuLiu Xue-ZhengWang Ting-Hua