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- Table of Contents
Facts about Holliday junction recognition protein.
Prevents CENPA-H4 tetramerization and prevents premature DNA binding from the CENPA-H4 tetramer. Directly binds Holliday junctions.
Human | |
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Gene Name: | HJURP |
Uniprot: | Q8NCD3 |
Entrez: | 55355 |
Belongs to: |
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No superfamily |
FAKTS14-3-3-associated AKT substrate; fetal liver expressing gene 1; Fetal liver-expressing gene 1 protein; FLEG1; hFLEG1; Holliday junction recognition protein; Up-regulated in lung cancer 9; URLC9DKFZp762E1312
Mass (kDA):
83.539 kDA
Human | |
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Location: | 2q37.1 |
Sequence: | 2; NC_000002.12 (233836701..233854566, complement) |
According to PubMed:17256767, highly expressed in the thymus with lower levels in the placenta, small intestine, liver, skeletal muscle, and colon. According to PubMed:17823411, highly expressed in testis, and at a relatively lower level in thymus and bone marrow. Significantly overexpressed in many lung cancer samples, compared with normal lung.
Nucleus, nucleolus. Chromosome, centromere. Localizes in centromeres during late telophase and early G1, when CENPA nucleosomes are assembled. Localizes to nucleolus during S phase, nucleolus site being often related to storage.
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In human primary cells, HJURP expression was downregulated after DNA damage induction, accelerating cellular senescence. HJURP can partially rescue cells from senescence. HJURP's role is still unknown.
HJURP has been studied in ovarian tumor cells. The expression of HJURP correlated with the level of the cancer cell marker MYC. HJURP, MYC, and MYC were also correlated when qRT-PCR was performed on 30 ovarian cancer tissues. Moreover, HJURP was also associated with the sensitivity of ovarian cancer cells to cisplatin.
HJURP is not only important for DSB repair but may also play a role in the metastatic process. HJURP knockdown resulted in A2780 cells losing their ability to invade and migrate, while HJURP expression increased these capabilities. HJURP has been linked to EMT. Knockdown of HJURP caused the inhibition of EMT markers. Vimentin and Slug were reduced in cells that had HJURP knockdown. However, HJURP upregulation resulted in poor prognosis.
The genes HJURP & WEE1 were identified in cell cultures that had been treated with siNC and siHJURP. The siRNAs were transfected into the cells with Lipofectamine 2000 (Thermo Fisher Scientific and Invitrogen) by transfection. Figure 3A depicts the GO enrichment of the two genes in the regulatory mechanism network. The number genes involved in the pathway's pathway is represented by their size. The color represents the relative -log10 of the pathway (P-adj. level. The selected terms of GO related to cell-cycle regulation were compared against the normal controls using log2FoldChange as a threshold. The Venn diagram was used as a visual aid to visualize the network.
These results indicate that HJURP contributes to DNA repair after cisplatin induced DNA damage. In a cisplatin-treated line of cells, HJURP knockdown reduced the speed of H2A.X. HJURP inhibitors and cisplatin DNA damage-induced DNA damage reduced gH2A.X levels, but these effects did not occur in HJURP knockdown cellular lines.
The Scm3/HJURP gene family is conserved in yeast and humans. It is proposed that it acts as CENP–A-specific chaperones. These proteins play a key role in CENPA loading. Although the exact mechanism of CENPA incorporation and maintenance is still not fully understood, it appears that several factors, such as HJURP marker, play a part. This study utilized a cell-free Xenopus egg system to assess the incorporation of CENP-A.
We used RNAi to determine if HJURP required CENPA's stable retention. We then combined it using pulse-chase experiments in order to confirm that CENPA-SNAP was stably retained by nucleosomes. We observed that CENP-A-SNAP was stable in all cells, regardless of the RNAi treatment. CENP-A–SNAP was found in both preincorporated and new pools as well as cells that had been RNAi-treated. There were no cellular changes.
HJURP can be disregarded in CENPA incorporation in Xenopus extracts. HJURP can't be used in stable retention of CENPA in Xenopus because it isn't able to compete with endogenous CENPA. This means that embryonic cells do not degrade exogenous CENPA.
For CENP A's recruitment into the centromeres it is essential that the CATD domain be maintained by CENP A. It is responsible for targeting CENP-A to centromeres. The HJURP protein binds CENP-A, and CENP-A subsequently induces centromeric nucleosomes. CENPA is thus able to maintain epigenetic stability and long-term stability.
A study using a SNAP-based fluorescent-pulse labeling method to analyze CENPA incorporation during the early G1 phase showed that CENPA has a distinct window. This window can be either a result of CENPA's intrinsic property or is associated to a general wave during G1 of histone exchanging at centromeres.
The Mis18BP1KNL2 role of the functional Eic1 gene in vertebrates, and fission yeast is equivalent. The Mis18 gene associates to the CCnp1CENPA subcomplex located at centromeres. Eic1 is essential for cell viability. HJURP does not allow stable retention of CENPA in fungi.
Recent studies have shown that drugs that target tumor-promoting gene genes may be developed using the HJURP gene. One such drug, called ionomycin D-triphosphate (ITDP), has been developed by GenePharma. GenePharma produces siRNA by using the sequences for two different genes HJURP/MYC. These siRNAs may be transiently injected into cells using either Tetrafectamine 2000 (Invitrogen), Lipofectamine 2000, or Tetrafectamine 2000. The siRNA sequences included siHJURP1 sense and siMYC antisense (both 5'-ACGGUGUGUGUGUAUAUAAUAAC).
Studies in the past have shown that HJURP genes play a role during malignant progression. This gene could be used to detect tumors. The protein is involved the the deposition CENPA at the centromere. Also, it is implicated for sensitivity to cisplatin during ovarian and cervical cancer. This protein could be a new target in combinatory therapy.
The HJURP cellular protein is a protein that is expressed mainly in the cytoplasm. The HJURP protein has been used to detect a variety of cancers, but its clinical application is still limited. In addition to the use of this gene as a tumor detection tool, HJURP can also help to identify other cancers that are closely related to HJURP.
A recent study revealed that HJURP can help detect early signs of various cancers including prostate and breast. The research is ongoing and further studies are needed to determine the effectiveness of this treatment. This research is critical for patients with advanced cancer. The authors recommend that physicians use the HJURP genetic test to diagnose a variety of cancers.
The cytoplasm is home to the HJURP genes. Boster Bio antibodies are highly specific, high-affinity, and have been cited for many years in scientific publications. They are also validated on Western Blotting, Immunohistochemistry, and ELISA. Boster offers a wide range of quality antibodies against HJURP.
Boster Bio HJURP markers are a great tool to help identify genes of interest. HJURP expression is high in the cytoplasmic of human cells. HJURP mediates the incorporation of CENP-A into chromatin in vertebrates. In humans, this protein forms a complex with acetylated histone H4. CENPA is coassembled with HJURP in the centromere to be deposited there.
Drosophila, like other dicots, has monocentric chromosomes. Homologues of the gene were also identified in humans. The CENH3-fused HJURP marker is predominantly expressed in the cytoplasm. It plays a role in transcription, mitosis and DNA synthesis.
PMID: 17823411 by Kato T., et al. Activation of Holliday junction recognizing protein involved in the chromosomal stability and immortality of cancer cells.
PMID: 16622419 by Foltz D.R., et al. The human CENP-A centromeric nucleosome-associated complex.