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Low false-positives in an mLumin-based bimolecular fluorescence complementation system with a bicistronic expression

Shun Liu1, Xiangyong Li2, Jie Yang3

  • 1Britton Chance Center for Biomedical Photonics, Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China. liushun@ibp.hust.edu.cn.

Sensors (Basel, Switzerland)
|February 22, 2014
PubMed
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This summary is machine-generated.

We developed the BEVL-BiFC system to improve the accuracy of bimolecular fluorescence complementation (BiFC) assays for studying protein-protein interactions (PPIs). This new system significantly reduces false positives, ensuring more reliable results in living cells.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Bimolecular fluorescence complementation (BiFC) is a sensitive technique for studying protein-protein interactions (PPIs) in living cells.
  • A major limitation of BiFC assays is the potential for non-specific association of fluorescent protein fragments, leading to false-positive results.
  • Accurate assessment of PPIs is crucial for understanding cellular processes and disease mechanisms.

Purpose of the Study:

  • To develop an improved BiFC system, termed BEVL-BiFC, that minimizes false-positive signals.
  • To enhance the reliability and accuracy of measuring PPIs in living cells.
  • To validate the BEVL-BiFC system using known protein interactions and investigate K-Ras interactions.

Main Methods:

  • Introduction of a bicistronic expression vector (pBudCE4.1) into an mLumin-based BiFC system to create the BEVL-BiFC system.

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  • Testing the BEVL-BiFC system with positive (Fos/Jun) and negative (ΔFos/Jun) controls to assess BiFC efficiency and false-positive rates.
  • Utilizing K-Ras and its interacting partners (Raf-1 RBD, Grb2) to confirm the system's accuracy and investigate specific interaction requirements.

    • Main Results:

    • The BEVL-BiFC system demonstrated a 25-fold contrast between positive and negative PPIs.
    • A low false-positive rate (<2% of cells) was observed in negative control experiments.
    • The system accurately revealed that K-Ras interaction with Raf-1 RBD is independent of post-translational modification and plasma membrane localization, while interaction with Grb2 requires K-Ras plasma membrane localization.

    Conclusions:

    • The developed BEVL-BiFC system effectively reduces the false-positive phenomenon common in traditional BiFC assays.
    • This enhanced system provides more robust and accurate measurements of protein-protein interactions in living cells.
    • The BEVL-BiFC system offers a valuable tool for precise PPI studies, contributing to a deeper understanding of molecular mechanisms.