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SMCX and components of the TIP60 complex contribute to E2 regulation of the HPV E6/E7 promoter

Jennifer A Smith1, Friederike S Haberstroh1, Elizabeth A White1

  • 1Department of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, United States.

Virology
|September 16, 2014
PubMed

Insights

Human papillomavirus (HPV) E2 protein recruits cellular proteins to repress viral oncogene expression. This mechanism involves histone modification, offering insights into HPV-associated lesion progression.

Area of Science:

  • Oncology
  • Molecular Biology
  • Virology

Background:

  • Malignant progression of HPV-associated lesions involves dysregulation of viral E6 and E7 oncogenes.
  • Loss of HPV E2 protein expression leads to increased E6/E7 expression.
  • Previous studies implicated Brd4, JARID1C/SMCX, and EP400 in E2-mediated repression.

Purpose of the Study:

  • To investigate the role of TIP60 histone acetyltransferase complex in HPV E2-mediated repression.
  • To further elucidate the mechanism of JARID1C/SMCX in E2-mediated repression.

Main Methods:

  • Investigated the contribution of TIP60 to E2 repression function.
  • Extended studies on SMCX function in HPV LCR regulation.
  • Analyzed histone H3K4 methylation marks in the presence of E2 and SMCX.

Main Results:

  • TIP60, a component of the TIP60/TRRAP complex, was found to contribute to E2 repression.
  • Di- and tri-methyl marks on histone H3K4 were reduced when E2 and SMCX were present.
  • These findings suggest a mechanism for SMCX in repressing the HPV LCR.

Conclusions:

  • HPV E2 protein recruits histone-modifying cellular proteins, including TIP60 and SMCX, to the HPV LCR.
  • Recruitment leads to transcriptional repression of viral E6 and E7 oncogenes.
  • This provides a molecular mechanism for controlling HPV oncogene expression and lesion progression.
Keywords:
ChromatinE2EP400H3K4LCRMethylationPapillomavirusSMCXTIP60Transcriptional repression

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