Journal
BIOCHEMISTRY
Volume 40, Issue 1, Pages 130-142Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi001881p
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Funding
- NIGMS NIH HHS [R01 GM059483, GM 52544] Funding Source: Medline
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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.
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