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GrainGenes Reference Report: PMB-26-1041

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Reference	PMB-26-1041
Title	Molecular characterization of the DNA-binding and dimerization domains of the bZIP transcription factor, EMBP-1
Journal	Plant Molecular Biology
Year	1994
Volume	26
Pages	1041-1053
Author	Guiltinan M Miller L
Abstract	The wheat basic-leucine zipper (bZIP) DNA-binding protein EmBP-1 has been implicated in the mechanisms of abscisic acid (ABA) mediated gene regulation Sequence and structural homology to the yeast bZIP protein GCN4 has been used to predict the location of the functional domains of EmBP-1 In order to test these predictions, the presumptive DNA-binding and dimerization domains of EmBP-1 were mapped by producing a series of truncated protein fragments and functionally testing them in vitro Deletion of 5 amino acids of the predicted basic domain resulted in a loss of all DNA-binding activity A fragment containing all six leucine repeat elements showed strong DNA-binding activity Sequential deletion of the leucine repeat elements resulted in first an increase in DNA-binding activity (-L6 and -L5) followed by a reduction in binding activity (-L4) and eventually complete elimination of all detectable DNA-binding activity (-L3 and -L2)
Keyword	amino acid sequence [ Show all 7 ]

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