Molecular and Cellular Biochemistry

, Volume 310, Issue 1–2, pp 49–55

Human tau protein forms complex with PrP and some GSS- and fCJD-related PrP mutants possess stronger binding activities with tau in vitro

  • Xiao-Fan Wang
  • Chen-Fang Dong
  • Jin Zhang
  • Yan-Zhen Wan
  • Feng Li
  • Yin-Xia Huang
  • Lu Han
  • Bing Shan
  • Chen Gao
  • Jun Han
  • Xiao-Ping Dong
Article

Abstract

Microtubule associated protein tau is considered to play roles in some types of human transmissible spongiform encephalopathies (TSE). In this study, the full-length and several truncated human tau proteins were expressed from E. coli and purified. Using GST pull down, co-immunoprecipitation assay and tau-coated ELISA, the molecular interaction between tau protein and PrP was confirmed in the context of the full-length human tau. The N terminus (amino acids 1–91) and tandem repeats region (amino acids 186–283) of tau protein were responsible for the interaction with PrP. The octapeptide repeats within PrP directly affected the binding activity of PrP with tau. GSS-related mutant PrP102L and fCJD- related mutants with two and seven extra octarepeats showed more active binding capacity with tau than wild-type PrP. The molecular interactions between PrP and tau protein highlight a potential role of tau in the biological function of PrP and the pathogenesis of TSE.

Keywords

Prion protein tau protein Transmissible spongiform encephalopathies 

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Copyright information

© Springer Science+Business Media, LLC. 2007

Authors and Affiliations

  • Xiao-Fan Wang
    • 1
  • Chen-Fang Dong
    • 1
  • Jin Zhang
    • 1
  • Yan-Zhen Wan
    • 1
  • Feng Li
    • 1
  • Yin-Xia Huang
    • 1
  • Lu Han
    • 1
  • Bing Shan
    • 1
  • Chen Gao
    • 1
  • Jun Han
    • 1
  • Xiao-Ping Dong
    • 1
  1. 1.State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and PreventionChinese Center for Disease Control and PreventionBeijingP.R. China

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