CHD3 (C-terminus) Monoclonal Antibody
- Known as:
- CHD3 (C-terminus) Monoclonal Antibody
- Catalog number:
- 27173
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- CHD3 (C-terminus) Monoclonal Antibody
Related genes to: CHD3 (C-terminus) Monoclonal Antibody
- Gene:
- CHD3 NIH gene
- Name:
- chromodomain helicase DNA binding protein 3
- Previous symbol:
- -
- Synonyms:
- Mi-2a, ZFH, Mi2-ALPHA
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-03-20
- Date modifiied:
- 2016-10-05
- Gene:
- SERBP1 NIH gene
- Name:
- SERPINE1 mRNA binding protein 1
- Previous symbol:
- -
- Synonyms:
- PAI-RBP1, DKFZP564M2423, CGI-55, HABP4L, PAIRBP1, CHD3IP
- Chromosome:
- 1p31.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-09-15
- Date modifiied:
- 2016-10-05
Related products to: CHD3 (C-terminus) Monoclonal Antibody
Related articles to: CHD3 (C-terminus) Monoclonal Antibody
- Suppression of human cytomegalovirus (HCMV) major immediate early gene (IE) expression from the viral major immediate early promoter (MIEP) is known to be crucial for the establishment and maintenance of HCMV latency in myeloid progenitor cells and their undifferentiated derivatives. This suppression of the MIEP during latent infection is known to result from epigenetic histone modification imparting a repressive chromatin structure around the MIEP in undifferentiated myeloid cells. In contrast, reactivation, resulting from, e.g., myeloid cell differentiation, is associated with activatory chromatin marks around the MIEP. Recently, recruitment of the transcriptional repressor SETDB1, KAP1, to latent HCMV genomes was shown to be involved in latency-associated MIEP suppression in CD34+ progenitor cells. KAP1 is also known to associate with Chromodomain-helicase-DNA-binding protein 3 (CHD3) as part of the NuRD complex which can aid transcriptional silencing. We now show that the cellular protein Plasminogen activator inhibitor 1 RNA-binding protein (SERBP1), a known interactor of CHD3, is significantly upregulated during HCMV latency and that this protein is required for MIEP suppression during latent infection of myeloid cells. We further show that SERBP1 mediates CHD3 association with the MIEP as well as KAP1 association with viral genomic DNA. We suggest that SERBP1 functions as a scaffold protein to recruit transcriptional repressors to the latent viral genome and to mediate transcriptional silencing of the MIEP during latent carriage. - Source: PubMed
Publication date: 2022/11/24
Poole EmmaSinclair John - The human protein CGI-55 has been described as a chromo-helicase-DNA-binding domain protein (CHD)-3 interacting protein and was also found to interact with the 3'-region of the plasminogen activator inhibitor (PAI)-1 mRNA. Here, we used CGI-55 as a "bait" in a yeast two-hybrid screen and identified eight interacting proteins: Daxx, Topoisomerase I binding RS (Topors), HPC2, UBA2, TDG, and protein inhibitor of activated STAT (signal transducer and activator of transcription) (PIAS)-1, -3, and -y. These proteins are either structurally or functionally associated with promyelocytic leukemia nuclear bodies (PML-NBs), protein sumoylation, or the regulation of transcription. The interactions of CGI-55 with Daxx, Topors, PIASy, and UBA2 were confirmed by in vivo colocalization experiments in HeLa cells, by using green (GFP) and red fluorescence fusion proteins. A mapping study of the CGI-55 binding site for these proteins revealed three distinct patterns of interaction. The fact that CGI-55-GFP has been localized in cytoplasm and nucleus in a dotted manner, and its interaction with proteins associated with PML-NBs, suggested that CGI-55 might be associated with nuclear bodies. Although Daxx and Topors co-localized with promyelocytic leukemia protein (PML), CGI-55 itself as well as PIASy and UBA2 showed only little co-localization with PML. However, we observed that CGI-55 localizes to the nucleolus and co-localizes with p80-coilin positive nuclear-coiled bodies. - Source: PubMed
Lemos Taíla AKobarg Jörg - The two human proteins Ki-1/57 and CGI-55 have highly similar amino acid sequences but their functions are unknown. We analyzed them by yeast two-hybrid screens and found that they interact with the C-terminal region of the human chromatin-remodeling factor CHD-3 (chromo-helicase-DNA-binding domain protein-3). The interaction of CGI-55 and CHD-3 could be confirmed in vitro and in vivo by co-immunoprecipitations from Sf9 insect cells. Mapping showed that CGI-55 interacts with CHD-3 via two regions at its N- and C-terminals. The CGI-55 and Ki-1/57 mRNAs show highest expression in muscle, colon and kidney. A CGI55-GFP fusion protein was localized in the cytoplasm, nucleus and perinuclear regions of HeLa cells. These data suggest the possibility that CGI-55 and Ki-1/57 might be involved in nuclear functions like the remodeling of chromatin. - Source: PubMed
Lemos Taíla APassos Dario ONery Flávia CKobarg Jörg