DNA specificity enhanced by sequential binding of protein monomers

Jennifer J. Kohler, Steven J. Metallo, Tanya L. Schneider, Alanna Schepartz

Research output: Contribution to journalArticle

87 Citations (Scopus)

Abstract

Transcriptional activation often requires the rapid assembly of complexes between dimeric transcription factors and specific DNA sites. Here we show that members of the basic region leucine zipper and basic region helix-loop-helix zipper transcription factor families follow an assembly pathway in which two protein monomers bind DNA sequentially and form their dimerization interface while bound to DNA. Nonspecific protein or DNA competitors have little effect on the rate of assembly along this pathway, but slow a competing pathway in which preformed dimers bind DNA. The sequential monomer-binding pathway allows the protein to search for and locate a specific DNA site more quickly, resulting in greater specificity prior to equilibrium.

Original languageEnglish (US)
Pages (from-to)11735-11739
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number21
DOIs
StatePublished - Oct 12 1999

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Carrier Proteins
DNA
Transcription Factors
Leucine Zippers
Proteins
Dimerization
Transcriptional Activation

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

DNA specificity enhanced by sequential binding of protein monomers. / Kohler, Jennifer J.; Metallo, Steven J.; Schneider, Tanya L.; Schepartz, Alanna.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 21, 12.10.1999, p. 11735-11739.

Research output: Contribution to journalArticle

Kohler, Jennifer J. ; Metallo, Steven J. ; Schneider, Tanya L. ; Schepartz, Alanna. / DNA specificity enhanced by sequential binding of protein monomers. In: Proceedings of the National Academy of Sciences of the United States of America. 1999 ; Vol. 96, No. 21. pp. 11735-11739.
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