Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A significant and global decrease in viral gene expression occurs with deletion of the carboxyl terminal domain of the human cytomegalovirus essential protein pUL34

ABSTRACT: The human cytomegalovirus UL34 gene encodes sequence-specific DNA-binding proteins and is essential for viral replication. Functionally, UL34 proteins (pUL34) repress expression of the viral immune evasion genes, US3 and US9. The amino terminal domain of pUL34 is sufficient for nuclear localization, DNA-binding and transcriptional repression. A virus lacking the entire carboxyl terminal of pUL34 was replication competent; however, deletion of the carboxyl terminal domain significantly impaired viral replication. There was a significant decrease in the transcription of viral genes at 4 hours post-infection following infection with the mutant virus which lacks the entire carboxyl terminal end of UL34 (UL34-COOH) relative to wild type virus, and an associated decrease in protein expression levels. Viral gene expression for the mutant virus was also decreased at 48 hpi but to a much smaller degree.

ORGANISM(S): Homo sapiens Human betaherpesvirus 5

PROVIDER: GSE106777 | GEO | 2019/11/10

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

A significant and global decrease in viral gene expression occurs with deletion of the carboxyl terminal domain of the human cytomegalovirus essential protein pUL34

Project description:A significant and global decrease in viral gene expression occurs with deletion of the carboxyl terminal domain of the human cytomegalovirus essential protein pUL34

| PRJNA417974 | ENA

CDK12 globally stimulates RNA polymerase II transcription elongation and carboxyl-terminal domain phosphorylation

Project description:CDK12 globally stimulates RNA polymerase II transcription elongation and carboxyl-terminal domain phosphorylation

| PRJNA550113 | ENA

CDK12 globally stimulates RNA polymerase II transcription elongation and carboxyl-terminal domain phosphorylation

Project description:CDK12 globally stimulates RNA polymerase II transcription elongation and carboxyl-terminal domain phosphorylation

| PRJNA474484 | ENA

CDK12 globally stimulates RNA polymerase II transcription elongation and carboxyl-terminal domain phosphorylation

Project description:Cyclin-dependent kinase 12 (CDK12) phosphorylates the carboxyl-terminal domain (CTD) of RNA polymerase II (pol II) but its roles in transcription beyond the expression of DNA damage response genes remain unclear. Here, we have used TT-seq and mNET-seq to monitor the direct effects of rapid CDK12 inhibition on transcription activity and CTD phosphorylation in human cells. CDK12 inhibition causes a genome-wide defect in transcription elongation and a global reduction of CTD Ser2 and Ser5 phosphorylation. The elongation defect is explained by the loss of the elongation factors LEO1 and CDC73, part of PAF1 complex, and SPT6 from the newly-elongating pol II. Our results indicate that CDK12 is a general activator of pol II transcription elongation and indicate that it targets both Ser2 and Ser5 residues of the pol II CTD.

2020-06-18 | GSE133156 | GEO

CDK12 globally stimulates RNA polymerase II transcription elongation and carboxyl-terminal domain phosphorylation

2020-06-03 | GSE115290 | GEO

Mapping the anti-cancer activity of α-connexin carboxyl-terminal (aCT1) peptide in resistant HER2+ breast cancer

Project description: This study aims to examine the mechanisms for the anti-cancer effects of a therapeutic peptide agent targeted to connexin 43 (Cx43) called alpha-connexin carboxyl-terminal peptide (aCT1). Findings from this study identify the effect of aCT1 on breast cancer signaling using a resistant HER2+ breast cancer cell line.

2023-12-20 | GSE250543 | GEO

The archaeal ATPase PINA interacts with the helicase Hjm via its carboxyl terminal KH domain remodeling and processing replication fork and Holliday junction

Project description:PINA is a novel ATPase and DNA helicase highly conserved in archaea, the third domain of life. The PINA from Sulfolobus islandicus (SisPINA) forms a hexameric ring, promotes Holliday junction (HJ) migration, and physically and functionally interacts with Hjc, the HJ specific endonuclease. Here, we show that SisPINA has strong physical interaction with Hjm (Hel308a), a helicase presumably targeting replication forks. In vitro biochemical analysis revealed that Hjm, Hjc, and SisPINA are able to coordinate HJ migration and cleavage in a concerted way. Deletion of the carboxyl 13 amino acid residues abolishes the interaction between SisPINA and Hjm. Crystal structure analysis showed that the carboxyl 70 amino acid residues fold into a type II KH domain which, in other proteins, functions in binding RNA and ssDNA. The KH domain not only mediates the interactions of PINA with Hjm and Hjc but also regulates the hexameric assembly of PINA. Our results collectively suggest possible mechanisms for SisPINA, Hjm, and Hjc to work together in replication fork regression, HJ formation, and HJ cleavage.

2018-10-22 | PXD008644 | Pride

Transcriptomic analysis of third instar larva wing imaginal discs deregulating Cyclin G in Drosophila melanogaster

Project description:We report here the transcriptomic analysis of Drosophila melanogaster wing imaginal discs from third instar female larvae expressing Cyclin G deleted of the PEST domain (the 25 COOH-terminal amin-acids) under the control of the daugterless-Gal4 ubiquitous driver. The negative control was transgenic flies wearing only the daugterless-Gal4 driver.

2017-07-01 | GSE99462 | GEO

Genome-wide binding of Cyclin G in Drosophila melanogaster third instar larva wing imaginal discs.

Project description:We describe here the genome-wide binding sites of Cyclin G in Drosophila melanogaster wing imaginal discs from third instar female larvae. We used a transgenic line expressing a version Cyclin G deleted of the PEST domain (the 25 COOH-terminal amin-acids) and tagged by Myc under the control of the daugterless-Gal4 ubiquitous driver.

2017-07-01 | GSE99461 | GEO

RNA-Seq analysis of wild-type and ttpA-D450trx mutant D. discoideum amebae

Project description:In many eukaryotes, mRNAs containing specific AU-rich motifs are regulated by proteins of the tristetraprolin (TTP) family, which bind to these motifs through a tandem zinc finger (TZF) domain. This binding leads to promotion of subsequent deadenylation and decay, partly through a conserved carboxyl-terminal CNOT1 binding domain. We explored the physiological role of the single TTP family member (TtpA) expressed in Dictyostelium discoideum. This study shows the effect of a carboxyl-terminal truncation (ttpA-D450trx), which removed the predicted CNOT1 binding domain, evaluated in amebae in growth medium during surface culture. The cells exhibited external and gene expression phenotypes that were very similar to those of two distinct null mutants, raising the possibility that this domain is necessary for TtpA-promoted mRNA decay in this species.

2021-11-24 | GSE156810 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data