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Functional Imaging of Viral Transcription Factories Using 3D Fluorescence Microscopy
09:03

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Published on: January 18, 2018

Viral transactivators specifically target distinct cellular protein kinases that phosphorylate the RNA polymerase II

C H Herrmann1, M O Gold, A P Rice

  • 1Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, USA.

Nucleic Acids Research
|February 1, 1996
PubMed

Insights

Viral transactivators like adenovirus E1A and herpes simplex virus VP16 interact with cellular CTD kinases, distinct from TAK. This interaction, crucial for transactivation, suggests multiple CTD kinases mediate viral responses.

Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Phosphorylation of RNA polymerase II's carboxyl-terminal domain (CTD) is vital for transcriptional regulation.
  • The human immunodeficiency virus transactivator Tat targets a cellular CTD kinase known as TAK.

Purpose of the Study:

  • To investigate interactions between other viral transactivators and cellular CTD kinases.
  • To determine if these interactions are relevant to transactivation functions.

Main Methods:

  • In vitro analysis of transactivator binding to CTD kinases.
  • Assessing kinase activity and specificity through biochemical assays.

Main Results:

  • Adenovirus E1A and herpes simplex virus VP16 proteins associate with CTD-hyperphosphorylating kinase activity.
  • This interaction requires functional activation domains of E1A and VP16.
  • The identified CTD kinase activities are distinct from TAK and MO15 (a component of TFIIH).

Conclusions:

  • Viral transactivators E1A and VP16 engage with distinct cellular CTD kinases.
  • These interactions are likely integral to their transactivation mechanisms.
  • At least two distinct CTD kinases may mediate cellular responses to viral transactivators.

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