Activation of protein kinase C inhibits adenovirus VA gene transcription in vitro

C B James1, T H Carter

  • 1Department of Biological Sciences, Ohio University, Athens 45701.

Insights

Activation of protein kinase C (PKC) inhibits adenovirus virus-associated (VA) gene transcription. This occurs because PKC activation prevents the VA gene from forming a stable transcription complex, as shown in vitro.

Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Adenovirus virus-associated (VA) genes are crucial for viral replication.
  • Protein kinase C (PKC) is a family of enzymes involved in various cellular signaling pathways.
  • Regulation of viral gene transcription is a key aspect of the viral life cycle.

Purpose of the Study:

  • To investigate the effect of protein kinase C (PKC) activation on adenovirus virus-associated (VA) gene transcription in vitro.
  • To elucidate the mechanism by which PKC influences VA gene transcription.

Main Methods:

  • In vitro transcription assays were performed using adenovirus DNA templates.
  • Protein kinase C (PKC) activity was modulated using activators (e.g., phosphatidyl serine) and inhibitors.
  • Cell extracts were used to study the formation of transcription complexes.

Main Results:

  • Activation of PKC led to the inhibition of adenovirus VA gene transcription in vitro.
  • PKC inhibitors restored transcription levels when phosphatidyl serine (PS) was present, indicating PKC involvement.
  • PKC activation prevented the formation of stable, initiated transcription complexes for VA genes.

Conclusions:

  • PKC activation plays an inhibitory role in adenovirus VA gene transcription.
  • The inhibition mechanism involves the disruption of transcription complex formation.
  • These findings provide insights into the regulation of viral gene expression by host cell kinases.

Related Concept Videos

Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
6.1K
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of...
7.7K
Eukaryotic Transcription Inhibitors01:52

Eukaryotic Transcription Inhibitors

Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells.
Eukaryotic transcription inhibitors usually contain two distinct domains, a...
11.1K
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
8.6K