DNA binding specificity of the wheat bZIP protein EmBP-1

EmBP-1 is a wheat DNA binding protein of the basic leucine zipper (bZIP) class of transcription factors implicated in the mechanisms of abscisic acid mediated gene activation. Understanding the role of EmBP-1 in regulating gene transcription requires elucidation of its DNA binding specificity. The b...

Full description

Saved in:
Bibliographic Details
Published in:Nucleic acids research 1994-11, Vol.22 (23), p.4969-4978
Main Authors: Niu, Xiping, Guiltinan, Mark J.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Basic-Leucine Zipper Transcription Factors
Binding Sites
Cloning, Molecular
DNA - metabolism
DNA, Complementary - genetics
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
G-Box Binding Factors
Gene Expression Regulation, Plant
Gene Library
Genes, Plant - genetics
Molecular Sequence Data
Polydeoxyribonucleotides - chemical synthesis
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - metabolism
Sequence Analysis, DNA
Transcription Factors
Transcription, Genetic - genetics
Transcriptional Activation
Triticum - genetics
Triticum aestivum
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:EmBP-1 is a wheat DNA binding protein of the basic leucine zipper (bZIP) class of transcription factors implicated in the mechanisms of abscisic acid mediated gene activation. Understanding the role of EmBP-1 in regulating gene transcription requires elucidation of its DNA binding specificity. The binding of EmBP-1 was studied using gel shift selection of DNA from random sequence pools. DNA binding sites were identified by sequencing of a selected pool and by cloning and sequencing individual sites. The binding sites were compared by mobility shift assay and DNase I footprinting, which show that EmBP-1 binds to a family of sequences with varying degrees of affinity. The highest affinity site bound by EmBP-1 is the palindrome GCCACGTGGC. EmBP-1 also binds several other sequences with high affinity, however most of these are asymmetric. While nearly all sequences bound by EmBP-1 contain an ACGT core sequence, EmBP-1 can also bind at least two sites with altered cores. These results provide a basis for comparing the DNA binding specificity of EmBP-1 with those of other plant bZIP proteins and provide insight into the possible target sites which EmBP-1 might bind in vivo.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/22.23.4969