TY  - BOOK
AU  - Niu,X.
AU  - Adams,C.C.
AU  - Workmaq,J.L.
AU  - Guiltinan,M.J.
TI  - Binding of the Wheat Basic Leucine Zipper Pmtein EmBP-1 to Nucleosomal Binding Sites 1s Modulated by Nucleosome Positioning
N2  - 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 a 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
UR  - https://drive.google.com/file/d/1BuavOKEzzPlhXC68Jmal95-8Wleg7bBZ/view?usp=drivesdk
ER  -