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- Table of Contents
Facts about Replication protein A 70 kDa DNA-binding subunit.
Thereby, it plays a vital role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation.
Human | |
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Gene Name: | RPA1 |
Uniprot: | P27694 |
Entrez: | 6117 |
Belongs to: |
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replication factor A protein 1 family |
HSSB; MST075; MSTP075; REPA1RF-A protein 1; Replication factor A protein 1; replication protein A 70 kDa DNA-binding subunit; replication protein A1 (70kD); replication protein A1, 70kDa; RF-A; RP-A; RPA70RP-A p70; Single-stranded DNA-binding protein
Mass (kDA):
68.138 kDA
Human | |
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Location: | 17p13.3 |
Sequence: | 17; NC_000017.11 (1830005..1900082) |
Nucleus. Nucleus, PML body. Enriched in PML bodies in cells displaying alternative lengthening of their telomeres.
The RPA1 gene is an important regulator of cell-mediated immunity. It is however lacking an entire N-terminus as well as a linker to allow localization. It is consequently located in the vicinity of its Nterminus. We will explore three of the most useful uses of RPA1 markers in this article. We also discuss the mutation t11 that is GFP-tagged, as well as the fragment containing the RPA2 coding region.
The RPA1 mutation is a unique, single-copy variant of human RPARPA. It alters the function of the gene, changing the way it interacts with other proteins. The mutation is linked to the protein's interactionwith other proteins, like CDKN1a. A three-year-old girl with hypogammaglobulinemia and lymphopenia, P4, was diagnosed with this mutation. Her disease was stable after IgG replacement therapy, however, her blood cells had a shorter telomere length than the normal range.
The mutation RPA1–t11 has been identified as a new molecular that plays a variety of functions in the cell. The mutations affect the ssDNA-binding function of the protein, however it is unclear if they influence the binding of DNA to RNA. This mutation may affect the ability of RPA to bind RNA to be affected, however it isn't being studied.
RPA1 mutant is not able to allow chromosomal replication. The mutant form has a decreased capacity to facilitate efficient priming of DNA polymerase beta and alpha in the presence of PCNA. In addition, the mutant RPA1 is not capable of supporting RAD51-dependent strand exchange. However the aRPA compound can promote RAD51-dependent strand exchange.
The mutation RPA1 has many beneficial effects. It binds Ddc2 and recruits the ATR-ATRIP complex to ssDNA. This mutation facilitates the phosphorylation substrates, which is a critical process in the checkpoint response. The mutation RPA1–t11 is a new way to evaluate the effectiveness of cancer treatments.
Acetylated histone (H3) is a crucial component of RNA polymerase II. To be able to understand how this protein affected by acetylated histone H3, a little background information is useful. RPAP1 is a new human RNA polymerase II-associated protein which has been purified affinity by using polymerase subunits made from recombinant DNA.
The RPA1 gene encodes the 70-kDa DNA-binding subunit. This protein is involved in several aspects of DNA metabolism, including chromosomal DNA replication, repair and recombination. It also plays a crucial function in maintaining telomeres and controlling the response of cells to DNA damage. Boster Bio: Best Uses For The RPA1 Marker
The RPA1-DFL gene mutation is a rare genetic variant that alters the gene's interaction with other proteins. It is associated with a higher susceptibility to coronary artery disease. It is also associated to decreased eNOS gene transcript. The mutation can be passed to the next generation. We know a lot about it. Boster Bio has identified three germline missense variants of RPA1 gene. All three are clustered to the DNA-binding domain of the RPA1 protein. RPA1 is a single-strand DNA-binding protein that is required for DNA replication and telomere preservation.
The mutation that causes RPA1–DFL recruitment of Ddc2, a DNA-binding protein, to the ssDNA. Zou and Elledge (2003, p. 101) The coated SsDNA is essential to recognize DNA damage and assists in phosphorylation of substrates as well as the activation of checkpoint signaling.
The RPA complex is composed of heterotrimeric proteins that bind to DNA single-stranded. These proteins play a significant role in the process of metabolism of DNA. They play a major role in DNA replication, recombination and telomere maintenance. They coordinate the cell's response to DNA injury. The most beneficial application of the RPA1-DFL mutation is to determine genes that cause apoptosis among patients.
The RPA1 marker gene is common in a variety of cells. The gene that encodes the protein has been used to identify more than 100 proteins. The RPA1 gene is responsible for the synthesis of a variety of proteins, including the cellular ER and senescence as well as the reticulocyte adhesion molecules. Its three subunits, RPA1, RPA2, RPA3 and RPA3 are found in a variety of cell kinds.
The RPA1 gene encodes the the replication protein A 70kDa. This protein is involved with DNA replication, telomere maintenance and repair of DNA. Its ssDNA binding function is vital to the cellular response to DNA damage. In addition the RPA complex can regulate the progression of cells and maintain telomeres. It is essential in DNA metabolism.
The gH2AX protein is phosphorylated whenever DNA damage occurs in cells. This marker was utilized in order to measure the degree of damage to DNA in mutant RPA1 cell lines. Its levels were significantly higher in mutant RPA1 cells that contained RPA1aroA or RPA1aroB. This suggests that the RPA1 gene plays a crucial role in controlling the cell cycle.
The subunit t11 of RPA1 is located in areas of DNA damage. While the N terminus of RPA1 is not crucial for recognizing DNA damage, it is required for DNA repair. Rad51 and RPA2 are essential for meiotic double-strand break processing. If both RPA1 and DBD-C exist, RPA1 can correct replication defects in RPA1-depleted cells.
The RPA family of single-stranded DNA binding proteins is vital for DNA replication, repair, recombination, cell cycle regulation, and a range of other functions. Previous studies have suggested that RPA levels can serve as biomarkers for different types of cancer. High RPA1 levels were linked to poor outcomes in esophageal carcinoma. These findings suggest that RPA mutations could be potential biomarkers for early diagnosis of GC.
Previous research has demonstrated that a lower expression level of RPA3 is linked to a poor prognosis for gastric cancers. However, less studies have explored whether RPA3 mutations can be used to predict gene expression in GC. Researchers from a team conducted an analysis of genetics to determine if RPA3 expression levels can be used to predict the outcome of patients in a recent study. The researchers conclude that their findings suggest the RPA family is associated with poor prognosis in a variety of cancer kinds.
In GC, the RPA3 gene can be found in normal samples. It is also associated with the survival rate. Patients with positive HER2 GC have a better chance of survival in the event of high expression of RPA3 in the normal sample. Patients with stage II GC have a lower chance of survival if RPA3 levels are low. Patients with advanced GC have a lower probability of surviving the long-term.
Studies have previously demonstrated that the presence of RPA2 in GC samples is associated with a favorable overall survival (OS) rate. The role of RPA2 in the prognostic aspect of GC remains unknown. No clinical trial has evaluated the specific prognostic value RPA2. Fortunately, an in-silico study has now characterized RPAs' prognostic as as immunological function in GC.
The study also found that the high expression of RPA3 mRNA was linked to a poorer overall survival (OS) rate. Patients suffering from diffuse GC and chronic GC were less likely to have a better OS when RPA3 levels were high. Patients receiving adjuvant treatment with 5-FU had a lower OS after RPA3 was increased.
Additionally, the study showed that a mutation in the RPA3 gene predicted the levels of genes in an HCC sample. However, further studies are needed to determine the exact function of this gene predicting the outcome of HCC. It will also assist in determining the best treatment options available to patients with the disease. If the gene RPA3 is involved in the progression of HCC the treatment must be determined accordingly.
The Oncomine database was used to examine the gene expression levels for RPA1 (and RPA2) in GC. In all three groups, the levels of RPA3 expression were significantly higher than in normal tissues. RPA4 levels were not significantly different between normal and GC groups. All authors are grateful for their contribution to this study. It is hoped that further research will increase the level of this gene accurate.
PMID: 2050703 by Erdile L.F., et al. Characterization of a cDNA encoding the 70-kDa single-stranded DNA- binding subunit of human replication protein A and the role of the protein in DNA replication.
PMID: 8420996 by Erdile L.F., et al. Type I human complement C2 deficiency. A 28-base pair gene deletion causes skipping of exon 6 during RNA splicing.