Binding of the wheat basic leucine zipper protein EmBP-1 to nucleosomal binding sites is modulated by nucleosome positioning

Xiping Niu, Christopher C. Adams, Jerry L. Workman, Mark J. Guiltinan

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

To investigate interactions of the basic leucine zipper transcription factor EmBP-1 with its recognition sites in nucleosomal DNA, we reconstituted an abscisic acid response element and a high-affinity binding site for EmBP-1 into human and wheat nucleosome cores in vitro. DNA binding studies demonstrated that nucleosomal elements can be bound by EmBP-1 at reduced affinities relative to naked DNA. EmBP-1 affinity was lowest when the recognition sites were positioned near the center of the nucleosome. Binding was achieved with a truncated DNA binding domain; however, binding of full-length EmBP-1 caused additional strong DNase I hypersensitivity flanking the binding sites. Similar results were observed with nucleosomes reconstituted with either human or wheat histones, demonstrating e conserved mechanism of transcription factor-nucleosome interactions. We conclude that positioning of recognition sequences on a nucleosome may play an important role in regulating interactions of EmBP-1 with its target sites in plant cells.

Original languageEnglish (US)
Pages (from-to)1569-1587
Number of pages19
JournalPlant Cell
Volume8
Issue number9
DOIs
StatePublished - Sep 1996

All Science Journal Classification (ASJC) codes

  • Plant Science
  • Cell Biology

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