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The early noncoding region of human papillomavirus type 16 is regulated by cytoplasmic polyadenylation factors

Jacob A Glahder1, Karen Kristiansen, Marjorie Durand

  • 1Department of Cellular and Molecular Medicine, Panum Institute, University of Copenhagen, DK-2200 Copenhagen N, Denmark. jglahder@hotmail.com

Virus Research
|February 11, 2010
PubMed

Insights

Human papillomavirus type 16 (HPV-16) early mRNAs utilize AU-rich sequences for polyadenylation. The human CPEB1 protein represses reporter gene activity, but this is counteracted by a fusion protein with hGLD-2.

Area of Science:

  • Molecular Biology
  • Virology
  • Gene Regulation

Background:

  • Human papillomavirus type 16 (HPV-16) early mRNAs are polyadenylated in the 3' untranslated region (3'UTR).
  • The HPV-16 3'UTR and early E5 open reading frame are AU-rich and contain five cytoplasmic polyadenylation element (CPE)-like regions.

Purpose of the Study:

  • To investigate the regulatory role of HPV-16 early 3' sequences in gene expression.
  • To determine the interaction of human CPEB1 and hGLD-2 with HPV-16 polyadenylation elements.

Main Methods:

  • Reporter gene assays were used to assess gene expression regulation.
  • A reporter construct containing HPV-16 early 3' sequences was created.
  • The effects of human CPEB1 and a hGLD-2/CPEB1 fusion protein were analyzed.

Main Results:

  • A fragment of the HPV-16 early 3' end, containing four CPE-like regions, conferred gene expression regulation when inserted downstream of a reporter gene.
  • Human CPEB1 repressed the activity of the reporter construct.
  • The hGLD-2/CPEB1 fusion protein counteracted CPEB1-mediated repression and facilitated poly(A) elongation of early HPV transcripts.

Conclusions:

  • The AU-rich regions in the HPV-16 early 3' end play a role in gene expression regulation.
  • CPEB1 and hGLD-2 are involved in the post-transcriptional regulation of HPV-16 early mRNAs.
  • The hGLD-2/CPEB1 fusion protein demonstrates potential in modulating HPV-16 transcript polyadenylation.

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