NUBP1 Antibody
- Known as:
- NUBP1 Antibody
- Catalog number:
- GWB-MU282C
- Product Quantity:
- 50ug
- Category:
- -
- Supplier:
- GenWay
- Gene target:
- NUBP1 Antibody
Related genes to: NUBP1 Antibody
- Gene:
- NUBP1 NIH gene
- Name:
- nucleotide binding protein 1
- Previous symbol:
- NBP1
- Synonyms:
- NBP35, CIAO5
- Chromosome:
- 16p13.13
- Locus Type:
- gene with protein product
- Date approved:
- 1998-07-03
- Date modifiied:
- 2018-05-17
Related products to: NUBP1 Antibody
Related articles to: NUBP1 Antibody
- Iron-sulfur (Fe-S) cluster assembly in the cytosol relies on coordinated transfer of [2Fe-2S] precursors to scaffold proteins of the cytosolic iron-sulfur assembly (CIA) machinery. Human glutaredoxin 3 (GLRX3) functions as a central [2Fe-2S] cluster donor and can form a heterotrimeric complex with the BolA-like protein BOLA2, whose functional role in cluster trafficking remains unclear. Here, we directly compare the cluster donor properties of the GLRX3 homodimer with those of the GLRX3-BOLA2 heterotrimer in the maturation of the CIA scaffold nucleotide-binding protein 1 (NUBP1). Using a combination of UV-Vis spectroscopy, acid-labile iron and sulfide quantification, circular dichroism kinetics, and paramagnetic NMR, we show that both complexes support assembly of a canonical [4Fe-4S] cluster on the N-terminal site of NUBP1. The structural and spectroscopic features of the assembled cluster are indistinguishable between the two donor systems, and comparable levels of cluster incorporation are observed. Kinetic analysis reveals that cluster transfer proceeds with similar apparent rate constants for GLRX3 and GLRX3-BOLA2 under glutathione-supported conditions. The presence of the physiological electron donor anamorsin accelerates the GLRX3-mediated transfer but does not significantly affect the kinetics of the GLRX3-BOLA2 system, suggesting a shift in the rate-limiting step upon BOLA2 association. Together, these results show that GLRX3-BOLA2 is fully competent for [2Fe-2S] cluster delivery to NUBP1 and supports the formation of the same final [4Fe-4S] cluster observed upon GLRX3-mediated transfer. Rather than enhancing transfer efficiency, BOLA2 association appears to play a nonkinetic role, potentially related to cluster stabilization by modulating the electron transfer process under specific cellular conditions. - Source: PubMed
Publication date: 2026/08/11
Masini MartinaCuccaro RosannaBanci Lucia - Ankylosing spondylitis (AS) and sarcopenia (SARC) often coexist, leading to impaired mobility through reduced muscle strength and altered bone metabolism. This study aimed to identify core diagnostic genes linking AS and SARC. This research analyzed 2 AS and 1 SARC dataset from the Gene Expression Omnibus database. Moreover, module genes and differentially expressed genes (DEGs) were evaluated via linear models for microarray data (Limma) and the weighted gene co-expression network analysis. Furthermore, functional enrichment analysis, various machine learning (ML) algorithms, and protein-protein interaction networks were employed for elucidating key candidate genes for the diagnosis of AS patients with SARC. The Receiver Operating Characteristic curve plots were utilized to determine the diagnostic significance of key genes. The merged AS dataset identified 1768 and 438 DEGs and module genes, respectively, in SARC. The intersection of module genes in SARC and DEGs in AS revealed 287 genes, which were predominantly enriched in oxidative phosphorylation. The protein-protein interaction network indicated 30 node genes. Furthermore, ML analysis identified 10 candidate hub genes for diagnostic value evaluation. In total, 6 candidate genes indicated high diagnostic significance key genes with the area under the curve > 0.7. The current study determined 6 hub genes (ENSA, FAM43A, MDH2, NUBP1, SAMM50, and TM2D1) for diagnosing AS patients with SARC, therefore providing a theoretical reference for potential diagnostic targets in these patients. - Source: PubMed
Ka YishaerLiu YingxinLi LanqiJiang HuiLv WenboWang LeiHe Xiaojin - Human cytosolic monothiol glutaredoxin-3 (GLRX3) plays a central role in the maturation of cytosolic [4Fe-4S] proteins by acting as a [2Fe-2S] cluster donor to early components of the cytosolic iron-sulfur assembly (CIA) machinery, including the P-loop NTPase nucleotide-binding protein 1 (NUBP1). While previous studies have established that dimeric, cluster-bridged GLRX3 transfers its [2Fe-2S] clusters to NUBP1 promoting the formation of the [4Fe-4S] cluster, the determinants within GLRX3 that enable this transfer remain unclear. Here, we analyze the specific contribution of each GLRX3 domain-glutaredoxin A (GrxA), glutaredoxin B (GrxB), and thioredoxin-like (Trx)-to the transfer of [2Fe-2S] clusters to NUBP1. We show in vitro that a cooperative mechanism between the two cluster-binding domains, GrxA and GrxB, is essential for the formation of a functional dimeric GLRX3 complex capable of efficient cluster transfer and for the assembly of the [4Fe-4S] cluster on NUBP1. In contrast, the Trx domain appears dispensable for this activity in these experimental conditions. These findings may provide new insights into the features underlying GLRX3 function in cytosolic [4Fe-4S] cluster biogenesis and highlight the domain-specific contributions to its role as a [2Fe-2S] cluster chaperone. - Source: PubMed
Publication date: 2025/10/10
Cuccaro RosannaMasini MartinaMalanho Silva JoséCamponeschi FrancescaBanci Lucia - In recent years, the dwindling population of these endangered geese has hindered our understanding of their phenotypic variations and the genes associated with important traits. To investigate the population structure and genetic diversity of this breed, the whole-genome data of 90 individuals from a conservation farm were obtained using the Illumina 6000 paired-end platform. The research results indicate that each locally endangered goose variety has formed a monophyletic population. The Baizi (BZ), Lingxian White (LX), and Xupu (XP) geese exhibiting higher genetic diversity than the other goose breeds. Tree-Mix analysis revealed the presence of five gene flows events between goose populations, with Yangjiang (YJ) geese consistently exhibiting significant genetic distance from the other breeds. Under strong pressures from the natural environment and artificial selection, whole-genome selective scanning revealed 394 overlapping genes. Gene Ontology (GO) enrichment analysis of the putative candidate genes (PCGs) revealed significant enrichment of 20 terms (P < 0.05). Similarly, Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analysis revealed significant enrichment of PCGs in 23 terms (P < 0.05). Examination of overlapping genes identified through at least two selection methods revealed a set of genes associated with key traits, including growth and development (CCND1, DES, CCNO, SMC5, and NUBP1), immunity (ABCA2, ABCC8, UHRF2, and ABCA1), and body aging (KAT6B). Our findings provide insights into the genetic basis of endangered geese at the whole-genome level, laying the foundation for future molecular research on genetic variation and phenotypic changes. In summary, our results provide invaluable resources for delineating the uniqueness of endangered goose breeds. - Source: PubMed
Publication date: 2025/03/08
Qi ShangzongWu TengWu HaoLiang YuZhao WenmingZhang YangXu QiChen Guohong - [4Fe-4S] cluster assembly in human cytosol requires both a [2Fe-2S] cluster chaperone being able to donate two [2Fe-2S] clusters and an electron donor providing two electrons to reductively couple the two [2Fe-2S] clusters into a [4Fe-4S] cluster. The mechanism through which the cytosolic [4Fe-4S] cluster assembly works is still not defined. Here, we show that a hetero-tetrameric complex formed by two molecules of cluster-reduced [2Fe-2S] -anamorsin and one molecule of dimeric cluster-oxidized [2Fe-2S] -GLRX3 orchestrates the assembly of a [4Fe-4S] cluster on the N-terminal cluster binding site of the cytosolic protein NUBP1. We demonstrate that the hetero-tetrameric complex is able to synergically provide two [2Fe-2S] clusters from GLRX3 and two electrons from anamorsin for the assembly of the [4Fe-4S] cluster on the N-terminal cluster binding site of NUBP1. We also showed that only one of the two [2Fe-2S] clusters bound to anamorsin, that is, that bound to the CX CX CXC motif, provides the electrons required to form the [4Fe-4S] cluster. Our study contributes to the molecular understanding of the mechanism of [4Fe-4S] protein biogenesis in the cytosol. - Source: PubMed
Bargagna BeatriceMatteucci SaraCiofi-Baffoni SimoneCamponeschi FrancescaBanci Lucia