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Removal of impurities from transcription factor preparations that alter their DNA-binding properties

Academic Article
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Overview

authors

  • Sun, L. P.
  • Kodadek, Thomas

publication date

  • 2002

journal

  • Nucleic Acids Research  Journal

abstract

  • Biochemical studies of transcriptional activators are important for understanding their detailed mechanism of action. Such experiments generally employ chimeric constructs comprised of fused DNA- binding and activation domains that are expressed in, and purified from, Escherichia coli, since full-length activators are usually difficult to express. We report here that such preparations contain chaperone impurities that affect the DNA-binding properties of the activator, for example sharply reducing the half-life of the protein-DNA complex. A simple method to remove these troublesome contaminants is described.

subject areas

  • Adenosine Triphosphate
  • Artifacts
  • Base Sequence
  • DNA
  • DNA-Binding Proteins
  • Electrophoretic Mobility Shift Assay
  • Half-Life
  • Kinetics
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins
  • Thermodynamics
  • Trans-Activators
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Identity

International Standard Serial Number (ISSN)

  • 0305-1048

Digital Object Identifier (DOI)

  • 10.1093/nar/gnf087

PubMed ID

  • 12177316
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Additional Document Info

start page

  • e88

volume

  • 30

issue

  • 16

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