Ask about this productRelated genes to: RFC5 Blocking Peptide
- Gene:
- RFC5 NIH gene
- Name:
- replication factor C subunit 5
- Previous symbol:
- -
- Synonyms:
- RFC36
- Chromosome:
- 12q24.23
- Locus Type:
- gene with protein product
- Date approved:
- 1994-10-14
- Date modifiied:
- 2016-10-05
Related products to: RFC5 Blocking Peptide
Related articles to: RFC5 Blocking Peptide
- In this study, we modeled gene expression profile data from Acute Myeloid Leukemia (AML) and healthy cases. At first, the GEO-GSE9476 dataset was processed, and a total of 341 genes were identified as differentially expressed genes (DEGs) in patients, and 599 DEGs in healthy individuals. Gene Ontology and pathway analysis on DEGs led to the identification of 5 Transcription Factors for patients and 3 for healthy cases. Analysis of the respective metabolic pathways revealed a common region in the metabolic pathway between AML and Tuberculosis (TB) that confirmed the validity of our procedure due to the consistency with similar reports. Upon PPI network analysis, Hub genes and three modules containing 41 up-regulated and down-regulated genes in AML patients were identified. Survival analysis on these genes results in reducing the number of identified effective genes into 3 upregulated (ITGAM, ITGAL and CD163) and 5 downregulated genes (MCM2, MCM3, RFC4, RFC5 and FEN1). Finally, drug sensitivity analysis was performed on these genes demonstrating complexity in drug-resistance due to the pattern of gene expression. This knowledge could potentially enable personalized treatment approaches based on individual patient responses due to the epigenetics and life style which affect gene expression pattern. - Source: PubMed
Publication date: 2026/07/27
Aghajan BehnamGhaemi Mohammad RezaMosammam Ali MHeshmati EmranKhalifeh Khosrow - Sliding clamps like PCNA are crucial processivity factors for replicative polymerases, requiring specific clamp loaders for loading onto DNA. The human alternative clamp loader CTF18-RFC interacts with the leading strand polymerase Pol ε and loads PCNA onto primer/template DNA using its RFC pentameric module. Here, we provide a structural characterization of the human CTF18-RFC complex and its interaction with PCNA. Our cryo-EM data support that the Ctf8 and Dcc1 subunits of CTF18-RFC, which form the regulatory module interacting with Pol ε, are flexibly tethered to the RFC module. A 2.9 Å cryo-EM structure shows the RFC module bound to PCNA in an autoinhibited conformation similar to the canonical RFC loader, marking the initial step of the clamp-loading reaction. The unique RFC1 (Ctf18) large subunit of CTF18-RFC, which based on the cryo-EM map shows high relative flexibility, is anchored to PCNA through an atypical low-affinity PIP box in the AAA+ domain and engages the RFC5 subunit using a novel β-hairpin at the disordered N-terminus. We show that deletion of this β-hairpin impairs the CTF18-RFC-PCNA complex stability, slows down clamp loading, and decreases the rate of primer synthesis by Pol ε. Our research identifies distinctive structural characteristics of the human CTF18-RFC complex, providing insights into its role in PCNA loading and the stimulation of leading strand synthesis by Pol ε. - Source: PubMed
Publication date: 2026/02/23
Briola Giuseppina RTehseen MohammadAl-Amodi AmaniYoung GraceDanazumi Ammar UNguyen Phong QuocSavva Christos GHedglin MarkHamdan Samir MDe Biasio Alfredo - Diffuse large B-cell lymphoma (DLBCL) is a heterogeneous disease that requires more reliable prognostic biomarkers. In this study, bioinformatic analysis identified replication factor C 5 (RFC5), one of the DNA repair-related gene, as a potential novel oncogene in DLBCL. Analysis of public datasets and immunohistochemical staining showed that RFC5 expression was significantly higher in tumor samples than in normal samples. High RFC5 expression was associated with worse prognostic clinical features. Notably, there was a difference in overall survival (OS) between the high- and low-RFC5 expression groups. Multivariate Cox regression analyses showed that RFC5 was an independent risk factor associated with poorer OS. Furthermore, correlations were observed between RFC5 expression in DLBCL and TIME(Tumor Immune Microenvironment), as well as immune cell infiltration, cytokine levels, cytokine receptor expression, and immune checkpoint activity. Gene set enrichment analysis (GSEA) analysis revealed that the elevated RFC5 expression group showed significant enrichment in multiple tumor signaling pathways. These results suggest that RFC5 may contribute to the pathogenesis of DLBCL by modulating these critical molecular pathways. Our findings indicate that RFC5 may be a novel prognostic biomarker for DLBCL. - Source: PubMed
Publication date: 2025/12/07
Tian ZuguoLiu ShuiyuWeng ChunlanRen Mingqiang - The capacity of tumor cells to repair DNA damage is closely associated with their resistance to radiotherapy and chemotherapy. Our investigation demonstrated elevated RFC5 levels within nasopharyngeal carcinoma (NPC) cells and is involved in DNA damage repair. Mechanistic studies revealed that high RFC5 expression in NPC cells reduces the formation of micronuclei during cisplatin treatment, thereby suppressing cGAS-STING signaling activation and limiting inflammatory mediator production, which in turn promotes tumor progression. In in vivo experiments, tumors with high RFC5 expression showed reduced secretion of IFN-γ and TNF-α by CD8T cells in the tumor immune microenvironment, along with enhanced PD-1, LAG-3, and CTLA-4 expression, leading to T cell exhaustion. Our findings suggest that RFC5 enhances the repair of cisplatin-induced DNA damage and promotes immune evasion, suggesting RFC5 is a promising therapeutic candidate for enhancing treatment outcomes in radiotherapy and chemotherapy. - Source: PubMed
Publication date: 2025/11/04
Han YumoMiao MengyuShan YingZhou YongPan SiZhu RuiYuan LingZhu ZiyuZhang Jie - Sliding clamps like PCNA are crucial processivity factors for replicative polymerases, requiring specific clamp loaders for loading onto DNA. The human alternative clamp loader CTF18-RFC interacts with the leading strand polymerase Pol ε and loads PCNA onto primer/template DNA using its RFC pentameric module. Here, we provide a structural characterization of the human CTF18-RFC complex and its interaction with PCNA. Our cryo-EM data support that the Ctf8 and Dcc1 subunits of CTF18-RFC, which form the regulatory module interacting with Pol ε, are flexibly tethered to the RFC module. A 2.9 Å cryo-EM structure shows the RFC module bound to PCNA in an autoinhibited conformation similar to the canonical RFC loader, marking the initial step of the clamp-loading reaction. The unique RFC1 (Ctf18) large subunit of CTF18-RFC, which based on the cryo-EM map shows high relative flexibility, is anchored to PCNA through an atypical low-affinity PIP box in the AAA+ domain and engages the RFC5 subunit using a novel β-hairpin at the disordered N-terminus. We show that deletion of this β-hairpin impairs the CTF18-RFC-PCNA complex stability, slows down clamp loading, and decreases the rate of primer synthesis by Pol ε. Our research identifies distinctive structural characteristics of the human CTF18-RFC complex, providing insights into its role in PCNA loading and the stimulation of leading strand synthesis by Pol ε. - Source: PubMed
Publication date: 2025/11/05
Briola Giuseppina RTehseen MuhammadAl-Amodi AmaniYoung GraceDanazumi Ammar UNguyen Phong QuocSavva Christos GHedglin MarkHamdan Samir MDe Biasio Alfredo