Partial Purification and Characterization of Two Transcription Factors, HBP-1a and HBP-1b, Specific for a cis-Acting Element, ACGTCA, of Wheat Histone Genes

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In wheat, the nuclear proteins HBP-1a and HBP-1b bind specifically to a hexameric motif ACGTCA which is essential for the efficient transcription of the gene for histone H3. The two factors were partially purified from wheat germ by sequential chromatography on columns of phosphocellulose, butyl-Sepharose and a specific DNA-affinity column. Differences were found between the partially purified HBP-1a and HBP-1b with respect to their DNA-binding properties. Treatment of the partially purified protein factors with alkaline phosphatase prevented the specific binding of DNA to HBP-1b but not to HBP-1a, suggesting that phosphorylation of HBP-1b may be involved in the regulation of its activity. Because the binding sites of HBP-1a and HBP-1b exhibit substantial overlap, their binding to the hexameric motif may be mutually exclusive. This possibility suggests that the interplay of these factors at the hexameric motif is important for the regulation of the transcription of the gene for histone H3.
日本植物生理学会の論文