The polyomavirus major capsid protein VP1 interacts with the nuclear matrix regulatory protein YY1

FEBS Lett. 2000 Feb 11;467(2-3):359-64. doi: 10.1016/s0014-5793(00)01170-4.

Abstract

Polyomavirus reaches the nucleus in a still encapsidated form, and the viral genome is readily found in association with the nuclear matrix. This association is thought to be essential for viral replication. In order to identify the protein(s) involved in the virus-nuclear matrix interaction, we focused on the possible roles exerted by the multifunctional cellular nuclear matrix protein Yin Yang 1 (YY1) and by the viral major capsid protein VP1. In the present work we report on the in vivo association between YY1 and VP1. Using the yeast two-hybrid system we demonstrate that the VP1 and YY1 proteins physically interact through the D-E region of VP1 and the activation domain of YY1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Viral / immunology
  • Capsid / genetics
  • Capsid / immunology
  • Capsid / metabolism*
  • Capsid Proteins*
  • Cell Extracts
  • Cell Line
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / immunology
  • DNA-Binding Proteins / metabolism*
  • Erythroid-Specific DNA-Binding Factors
  • Mice
  • Mutation
  • Nuclear Proteins / metabolism*
  • Polyomavirus / physiology*
  • Precipitin Tests
  • Saccharomyces cerevisiae
  • Transcription Factors / genetics
  • Transcription Factors / immunology
  • Transcription Factors / metabolism*
  • Transfection
  • Two-Hybrid System Techniques
  • Virus Replication / physiology
  • YY1 Transcription Factor

Substances

  • Antibodies, Viral
  • Capsid Proteins
  • Cell Extracts
  • DNA-Binding Proteins
  • Erythroid-Specific DNA-Binding Factors
  • Nuclear Proteins
  • Transcription Factors
  • VP1 protein, polyomavirus
  • YY1 Transcription Factor
  • Yy1 protein, mouse