Ecopipet spare part and service kit
- Known as:
- Ecopipet spare service reagent
- Catalog number:
- SKE-01
- Category:
- -
- Supplier:
- Capp
- Gene target:
- Ecopipet spare part and service kit
Related genes to: Ecopipet spare part and service kit
- Gene:
- SPRTN NIH gene
- Name:
- SprT-like N-terminal domain
- Previous symbol:
- C1orf124
- Synonyms:
- DKFZP547N043, Spartan, DVC1
- Chromosome:
- 1q42.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-06-23
- Date modifiied:
- 2016-10-18
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- DNA polymerase ζ (Polζ) is essential for replication across damaged DNA, yet the mechanisms governing its regulation in mammalian cells remain incompletely understood. The catalytic subunit REV3L is nearly twice the size of its yeast counterpart owing to a large vertebrate-specific insertion, and recent studies reported that REV3L undergoes proteolytic cleavage by the endopeptidase TASP1. Here, we show that REV3L cleavage generates two stable fragments, Nter-p70 and Cter-p300, which reassociate into a long-lived heterodimeric complex with enhanced polymerase activity. This interaction is stabilized by key residues within the catalytically inactive EXO domain. The cleaved Polζ complex associates with chromatin, binds nascent DNA, and undergoes ATR-dependent phosphorylation in response to replication stress. Importantly, preventing REV3L cleavage markedly impairs Polζ activity, reduces cisplatin-induced mutagenesis, and increases RAD51 nuclear foci and sister chromatid exchange, consistent with a compensatory shift toward homologous recombination-mediated repair. Together, our findings suggest that the vertebrate-specific expansion of REV3L necessitated cleavage to restore structural organization and optimize catalytic function, representing an evolutionary adaptation in DNA damage tolerance pathways. - Source: PubMed
Publication date: 2026/06/15
Goulas JordaneGuignier BasileBen Yamin BarbaraPouvelle CarolineYurchenko AndreyDespras Emmanuellede Oliveira LucianaLaplante PierreBochaton DorianPlassard DamienYang WeiTheillet François-XavierVeaute XavierWood Richard DNikolaev SergeyCordonnier Agnès MKannouche Patricia L - Topoisomerase 1 (TOP1) is essential for relieving DNA supercoils during replication and transcription. However, its transient reaction intermediates (TOP1 cleavage complexes or TOP1-DNA covalent complexes, i.e., TOP1ccs) become highly genotoxic when stabilized. While mechanisms that resolve chemotherapy-induced TOP1ccs are well-characterized, how cells prevent their accumulation under physiological conditions for securing genomic stability has remained elusive. Here, we elucidate a novel regulatory pathway in which CHK1-mediated phosphorylation of TOP1 at Serine-320 regulates its religation activity and hence limits steady-state TOP1cc levels during unperturbed cellular metabolism. We further demonstrate a distinct mechanism of TOP1cc stabilization, which escapes recognition by proteasomal and autophagic machineries, while being susceptible to CtIP, SPRTN, and p97-mediated removal. Defective phosphorylation of TOP1 at S320 impairs replication-fork progression, leading to replication- and transcription-associated DSBs, R-loop stabilization, genomic instability, and hypersensitivity to TOP1 poisons. Overall, our study assigns a new function to CHK1 in direct regulation of human TOP1cc dynamics, with critical implications for genomic integrity and combinatorial chemotherapy. - Source: PubMed
Publication date: 2026/05/13
Guha Majumdar AnandaChauhan NitishGupta PoojaSubramanian MaheshPatro Birija Sankar - The DNA-dependent metalloprotease SPRTN has emerged as a key enzyme in the proteolysis of DNA-protein crosslinks (DPCs), thereby protecting us against genome instability, accelerated ageing, and cancer. DNA and ubiquitin chains serve as the primary activator and catalyst of SPRTN proteolysis, respectively, but how they promote SPRTN activation and activity remains incompletely understood. To address this question, we developed a highly sensitive multi-turnover fluorescence resonance energy transfer (FRET) assay to monitor SPRTN proteolysis in real time. We found that the auto-cleaved N-terminal SPRTN fragment, comprising the metalloprotease domain (MPD), zinc-binding domain (ZBD), and basic region (BR), is highly stable, enzymatically active, and retains ubiquitin-dependent activation. Interestingly, the MPD alone exhibits basal intrinsic activity that is independent of both DNA activation and ubiquitin avidity effect. We show that ZBD and MPD together exert steric regulation: ZBD maintains MPD in an autoinhibited state, while MPD largely prevents ZBD from binding to DNA. BR, together with DNA, is essential to relieve ZBD-mediated inhibition of MPD. Using a site-trapping approach, we demonstrate that the ZBD-BR- DNA trinity induces an open conformation of the SPRTN N-terminus in cis, thereby releasing autoinhibition. MPD and BR together restrict the DNA-binding stoichiometry of ZBD, enabling SPRTN to function efficiently in proximity to DNA despite its low abundance in vivo. Collectively, our work overturns the long-standing dogma that SPRTN autocleavage inactivates the enzyme and reveals how DNA-induced conformational changes in SPRTN fine-tune its protease activity, providing a prerequisite for subsequent ubiquitin activation and rapid proteolysis of DPCs. - Source: PubMed
Publication date: 2026/05/01
Song WeiNewman Joseph AZhao YichenChalk RodRedfield ChristinaElliott Paul RRamadan Kristijan - DNA-protein cross-links (DPCs) represent a prevalent form of DNA damage that forms when cellular proteins become covalently trapped to DNA strands upon exposure to various endogenous and exogenous agents. Methylglyoxal is an endogenous metabolite that reacts with guanine and adenine bases in DNA and RNA, as well as cysteine, arginine, and lysine residues in proteins, generating advanced glycation end-products (AGEs), including DPCs. These modifications have been linked to human disease, including cancer, liver disease, diabetes, and neurodegenerative disorders. Herein, we present a mass spectrometry method for quantifying MGO-induced DNA-protein cross-links (DPCs) in human cells. We prepared an isotope NC-dG-MGO-Lys internal standard and developed a quantitative liquid chromatography-tandem mass spectrometry (LC-MS/MS) method for detecting and quantifying the formation and repair of dG-MGO-Lys DPCs in cells. Genomic DNA was extracted, subjected to sequential protease and nuclease digestion, purified by offline high-performance liquid chromatography (HPLC), and analyzed by LC-MS/MS. The method's standard curve showed a strong linear relationship across a concentration range of 10-1000 fmol ( = 0.9994). The method achieved limits of detection (LOD) and quantification (LOQ) of 10 and 20 fmol, respectively. Inhibition of proteasome and SPRTN activity revealed that SPRTN functions as a predominant proteolytic enzyme in MGO DPC repair. Overall, this analytical approach can offer valuable insights into the relevance of DPCs in diseases linked to elevated MGO levels. - Source: PubMed
Publication date: 2026/04/17
Omondi Reinner OBarnes Elijah MGurajala Krishna CFisette GabrielleChaudray Ibaad AErber Luke - Oxidative DNA damage caused by endogenous reactive oxygen species (ROS) is a key driver of mutagenesis, cellular dysfunction, and aging, contributing to diseases like cancer, neurodegeneration, rheumatoid arthritis, cardiovascular disorders, and diabetes. Although more than 20 oxidative base lesions have been identified, ROS-induced DNA-protein crosslinks (DPCs) are poorly characterized. ROS-DPCs are unusually bulky and highly toxic lesions that accumulate in metabolically active tissues with age, but their identities, biological consequences, and repair in living cells have remained elusive. In the present work, we characterized ROS-DPCs in human fibrosarcoma (HT1080) cells treated with hydrogen peroxide (HO) and elucidated the mechanisms of their removal. Mass spectrometry-based proteomics has identified over 100 cellular proteins that participated in DPC formation, most of which are involved in DNA metabolism. Our data further reveal that DNA replication and transcription facilitate DPC detection and identify a critical role of the ubiquitin-proteasomal system (UPS), replication-coupled activity of SPRTN metalloprotease, and nucleotide excision repair (NER) in removing ROS-induced DPCs. ROS-DPC formation was blocked by pretreatment with metabolically stable and cell-permeable glutathione (GSH) analog (Ψ-GSH), suggesting a possible therapeutic strategy for preventing diseases associated with increased ROS levels. - Source: PubMed
Publication date: 2026/03/13
Cyuzuzo Cesar IKruk MonicaZhang QiAlshareef DuhaHarmon JamesMachida Yuichi JVanKoten Harrison WMore Swati SCampbell ColinTretyakova Natalia Y