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Adenovirus precursor pVII protein stability is regulated by its propeptide sequence

Raviteja Inturi1, Srinivas Thaduri, Tanel Punga

  • 1Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden.

Plos One
|November 22, 2013
PubMed

Insights

The adenovirus pVII protein precursor

Area of Science:

  • Molecular biology
  • Virology
  • Cellular biology

Background:

  • Adenovirus encodes the pVII protein, crucial for viral DNA structure.
  • pVII protein is synthesized as a precursor requiring proteolytic processing.
  • The propeptide sequence's function in precursor pVII protein regulation is unclear.

Purpose of the Study:

  • To elucidate the molecular functions of the propeptide sequence in the precursor pVII protein.
  • To investigate the role of the propeptide in precursor pVII protein stability and degradation.
  • To explore the involvement of the Cullin-3 E3 ubiquitin ligase complex in this process.

Main Methods:

  • Proteasomal degradation assays.
  • Analysis of precursor pVII protein stability.
  • Investigation of Cullin-3 E3 ubiquitin ligase complex interactions.
  • Adenovirus gene expression analysis.

Main Results:

  • The propeptide targets precursor pVII protein for proteasomal degradation.
  • Propeptide and lysine residues K26/K27 co-dependently regulate precursor pVII protein stability.
  • Cullin-3 E3 ubiquitin ligase complex associates with the propeptide, affecting precursor pVII protein stability.
  • Inactivation of Cullin-3 reduces early adenovirus E1A gene expression.

Conclusions:

  • The adenovirus propeptide sequence has a novel function in targeting precursor pVII protein for degradation.
  • Cullin-3 E3 ubiquitin ligase complex plays a role in regulating precursor pVII protein stability.
  • Cullin-3 is involved in modulating adenovirus gene expression during early infection.

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