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Related Experiment Videos

Patch clamp and atomic force microscopy demonstrate TATA-binding protein (TBP) interactions with the nuclear pore

J O Bustamante1, A Liepins, R A Prendergast

  • 1University of Maryland School of Medicine, Department of Physiology, Baltimore 21201, USA.

The Journal of Membrane Biology
|August 1, 1995
PubMed
Summary

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The TATA-binding protein (TBP) regulates nuclear pore complex (NPC) transport, impacting gene expression. TBP modifies NPC structure and function, potentially opening channels and stabilizing NPCs for cellular processes.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biophysics

Background:

  • TATA-binding protein (TBP) is crucial for RNA polymerase II transcription via the TFIID complex.
  • TBP's size suggests nuclear pore complexes (NPCs) might limit its nuclear entry.

Purpose of the Study:

  • To investigate NPC regulation of TBP translocation into the nucleus.
  • To determine TBP's effects on NPC structure and function.

Main Methods:

  • Patch-clamp electrophysiology to measure NPC channel conductance.
  • Atomic force microscopy (AFM) to visualize TBP interaction with NPCs.

Main Results:

  • NPCs regulate TBP movement; translocation is ATP-dependent.
  • TBP transiently plugs NPC channels, reducing conductance.

Related Experiment Videos

  • High TBP concentrations (>250 pM) cause permanent NPC channel opening.
  • AFM shows TBP accumulation on the NPC cytosolic side.

    • Conclusions:

    • TBP stabilizes NPCs, induces permanent channel opening, and increases functional channels.
    • TBP's interaction with NPCs offers new insights into gene expression regulation.
    • Findings are relevant to normal and pathological cellular mechanisms.