Nagk siRNA_Lentivectors
- Known as:
- Nagk siRNA_Lentivectors
- Catalog number:
- i064169c
- Product Quantity:
- 500ng
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Nagk siRNA_Lentivectors
Related genes to: Nagk siRNA_Lentivectors
- Gene:
- NAGK NIH gene
- Name:
- N-acetylglucosamine kinase
- Previous symbol:
- -
- Synonyms:
- GNK
- Chromosome:
- 2p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-11-16
- Date modifiied:
- 2016-04-25
Related products to: Nagk siRNA_Lentivectors
Related articles to: Nagk siRNA_Lentivectors
- Fluorescence hybridization (FISH) is commonly used to detect the copy number (M/N ratio) in postoperative or biopsy-derived neuroblastoma (NB) tissue samples, a critical indicator for risk stratification of NB. However, most NB patients present with large tumors at an advanced stage, making tissue acquisition difficult both surgically and biopsy. Therefore, a triple-amplified sequential activation allosteric DNA biosensor, termed TASA (comprising -TASA and -TASA), which leverages the elevated enzymatic activities of apurinic/apyrimidinic endonuclease 1 (APE1) and telomerase in the cytoplasm of NB cells as molecular switches and signal amplification molecules, was developed for quantitative detection of the M/N ratio of NB. -TASA and -TASA sequentially interact with APE1, (or ), and telomerase, undergoing a conformational change that cyclically separates the fluorophore from the quencher with high efficiency, thereby producing a detectable fluorescence signal. -TASA and -TASA exhibit superior sensitivity, with limits of detection of 0.45 aM and 0.75 aM for mRNA and mRNA, respectively. In addition, -TASA and -TASA enable rapid quantitative determination of the M/N ratio in NB tissues. In particular, -TASA and -TASA enable accurate quantification of the M/N ratio in clinical NB tissues. In summary, this study presents a novel strategy for quantifying the NB M/N ratio, demonstrating significant potential for future applications in biomedical research and clinical diagnosis. - Source: PubMed
Publication date: 2026/07/16
Zhao LiangZhang YingyuTian HengyunZhang MengxinLiu KangboSun MengLi ZirongHou LigongZhang XianweiZhang Wancun - Bacterial peptidoglycan fragments (PGNs) are pathogen-associated molecular patterns that activate the mammalian innate immune system, particularly through NOD2 signaling pathways. Since NOD2 is a cytosolic sensor in mammalian cells, cellular assays are commonly used to identify bioactive PGNs that elicit NOD2 response, with muramyl dipeptide (MDP) long recognized as the minimal NOD2 agonist. However, recent studies have highlighted the intracellular phosphorylation of MDP by mammalian -acetylglucosamine kinase (NAGK) as a critical prerequisite for NOD2 activation, emphasizing the need for further investigation into other host-mediated processing of PGNs. In this study, we examined how various bacterial PGNs, differing in saccharide and stem peptide length, undergo intracellular structural modifications within mammalian cells. Our findings show that disaccharide PGNs are processed through intracellular glycosidic cleavage to generate monosaccharide MurNAc-containing PGNs intracellularly, followed by NAGK-dependent phosphorylation, uncovering an additional essential step that precedes NOD2 activation. To identify the glycosidase responsible for disaccharide PGN cleavage, we provide biochemical and cellular observations that human -GlcNAcase functions as a promiscuous glycosidase capable of processing certain disaccharide PGNs and potentially modulate their NOD2 activation. Furthermore, we demonstrate that PGNs with a lysine-type tripeptide stem are specifically cleaved into dipeptides and that phosphorylated PGNs are subjected to dephosphorylation in mammalian cells. Together, these findings offer insights into the metabolism and intracellular processing of PGNs in mammalian cells, which are crucial in shaping the host innate immune responses. - Source: PubMed
Publication date: 2026/07/07
Feng ShiliuAdamson ChristopherLi ChenyuNg Evan Wei LongQiao Yuan - Arginine is a semi-essential amino acid and holds significant value in the pharmaceutical and nutraceutical industries. Corynebacterium glutamicum is a promising host for arginine production, yet its industrial titers remain limited. Biosensor-based high-throughput screening enables rapid isolation of overproducers. However, the native LysG-based biosensor in C. glutamicum lacks arginine specificity, limiting its efficiency for screening high arginine-producing strains. Here, we developed an arginine-specific biosensor pLysG in C. glutamicum, by combining semi-rational design and directed evolution of LysG, an endogenous regulator responsive to basic amino acids. Structural and interaction analyses revealed that the F222I substitution in LysG retained high affinity for arginine while significantly decreasing its responsiveness to histidine and lysine. Subsequently, this arginine-specific biosensor was successfully applied to screen a library of N-acetylglutamate kinase (NAGK) mutants, identifying 18 novel NAGK mutants with enhanced arginine production compared with previously reported variants. The strain integrated with the optimal NAGK mutant was further subjected to mutagenesis and screening, yielding an engineered strain that achieved an arginine titer of 56.07 g/L in a 5-L bioreactor, a 42% increase relative to the original starting strain. Overall, this study provides a powerful tool for accelerating the metabolic engineering of C. glutamicum for high-level arginine production. - Source: PubMed
Publication date: 2026/05/25
Cai NingyunWang YeRen PengchengRao DemingShi TuoWang ZiyaoShen JieZhou WenjuanQi LinlinWang LixianChen NingChen JiuzhouZheng PingSun Jibin - PII protein is widely acknowledged to regulate intracellular nitrogen and carbon metabolism by interacting with several crucial proteins. N-acetyl-L-glutamate kinase (NAGK), a rate-limiting enzyme for arginine biosynthesis, is regarded as a potential target of PII protein. Nevertheless, the regulatory function remains ambiguous in green algae and has not been investigated in Haematococcus pluvialis. In this study, the NAGK enzyme and PII protein of H. pluvialis (designated as HpNAGK and HpPII, respectively) and their interaction relationships were characterized. The results indicated that HpNAGK showed high similarity with the same enzyme in the green algae. A subcellular localization assay indicated that both HpPII and HpNAGK were located in the chloroplasts. Yeast two-hybrid, pull-down, and bimolecular fluorescence complementation assays distinctly verified the interaction between HpPII and HpNAGK, which occurs in the chloroplasts. The structure of the HpPII-HpNAGK complex was predicted through docking analysis. Moreover, the HpNAGK activity was significantly enhanced by HpPII in the presence of glutamine in vitro. Under nitrogen starvation, HpNAGK activity declined in vivo, concomitant with a reduction in arginine accumulation. The regulatory function of HpPII on HpNAGK activity aligned with that in Chlamydomonas reinhardtii but differed from that in Dunaliella salina, suggesting species specificity among green algae. These findings provide insights into the regulatory function of PII protein in green algae and help to unveil the response mechanisms of H. pluvialis to different nitrogen statuses. - Source: PubMed
Publication date: 2026/04/18
Ma RuijuanChen ZiyueLiu JunjieMeng XingTao XinyiChen YuchengZhang ChunxiaoWang LingLu KangleLi XueshanSong KaiChen JianfengXie Youping - BACKGROUND: Beta-lactams are among the most successful antibiotics for treating bacterial infections, but its use is impeded by increasing resistance. The contribution of BlrAB and CreBC two-component regulatory systems (TCSs) to β-lactam resistance is reported in Aeromonas spp. and Pseudomonas aeruginosa, respectively. Stenotrophomonas maltophilia, an opportunistic pathogen, is resistant to most β-lactams due to the chromosomally encoded β-lactamases L1 and L2. The role of CreBC TCS in the β-lactam resistance of S. maltophilia is still unclear. In this article, we aimed to address this issue. RESULTS: The susceptibility of KJΔBC, a creBC mutant of S. maltophilia KJ, to ceftazidime (CAZ) and ticarcillin-clavulanate increased compared to that of the wild-type KJ. Consistently, the CAZ-induced β-lactamase activity of KJΔBC was lower than that of the wild-type KJ. To find out the candidate responsible for the ΔcreBC-mediated β-lactam susceptibility increase and β-lactamase activity decrease, transcriptome results of wild-type KJ and KJΔBC were analyzed, focusing on the genes whose encoding proteins are involved in peptidoglycan (PG) homeostasis. Among the genes surveyed, anmK was the highest upregulated in KJΔBC. anmK encodes an anhydro-N-acetylmuramic acid kinase, which converts anhMurNAc to MurNAc-6P in the PG recycling pathway. The anmK gene and its upstream gene Smlt0416 (annotated as anmH) formed a two-member operon. Promoter activity of anmHK operon was upregulated in KJΔBC. However, the CAZ challenge hardly altered creBC and anmHK operons expression. anmK, but not anmH, deletion from the KJΔBC chromosome reverted CAZ resistance and CAZ-induced β-lactamase activity to the wild-type level. CONCLUSIONS: In unstressed S. maltophilia, CreBC TCS is activated and partially represses anmHK operon, favoring PG recycling toward the NagK-dependent pathway. In the CAZ-treated creBC mutant, anmHK operon is derepressed and the elevated AnmK activity may enhance the AnmK–MupP–AmgK–MurU–MurCDEF pathway, thereby increasing UDP-MurNAc-pentapeptide levels and decreasing β-lactam-induced β-lactamase activity. A creBC–anmK–L1/L2 regulatory circuit responsible for CAZ resistance has been established in S. maltophilia. - Source: PubMed
Publication date: 2026/04/16
Yang Tsuey-ChingLu Hsu-FengWu Chao-JungHu En-WeiLu Yu-LiangLi Li-Hua