Kinetic studies of Fos·Jun·DNA complex formation: DNA binding prior to dimerization

J. J. Kohler, A. Schepartz

Research output: Contribution to journalArticle

93 Citations (Scopus)

Abstract

The bZIP proteins Fos and Jun bind DNA rapidly and with high affinity, forming a heteromeric complex that mediates activated transcription. Here we use stopped-flow fluorescence resonance energy transfer (FRET) to study the kinetic pathway by which Fos·Jun·DNA complexes assemble. Though dimerization of Fos and Jun occurs rapidly in the absence of DNA, the rate of dimerization is enhanced in the presence of DNA. Global analysis of the kinetic data shows that the favored DNA binding pathway is one is which the two protein monomers bind DNA sequentially and assemble their dimerization interface while bound to DNA.

Original languageEnglish (US)
Pages (from-to)130-142
Number of pages13
JournalBiochemistry
Volume40
Issue number1
DOIs
StatePublished - Jan 9 2001

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Dimerization
Kinetics
DNA
Basic-Leucine Zipper Transcription Factors
Fluorescence Resonance Energy Transfer
Transcription
Monomers
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kinetic studies of Fos·Jun·DNA complex formation : DNA binding prior to dimerization. / Kohler, J. J.; Schepartz, A.

In: Biochemistry, Vol. 40, No. 1, 09.01.2001, p. 130-142.

Research output: Contribution to journalArticle

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