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Science 1 September 1989:
Vol. 245. no. 4921, pp. 965 - 967
DOI: 10.1126/science.2772648

Articles

Science, Vol 245, Issue 4921, 965-967
Copyright © 1989 by American Association for the Advancement of Science


articles

A protein that binds to a cis-acting element of wheat histone genes has a leucine zipper motif

T Tabata, H Takase, S Takayama, K Mikami, A Nakatsuka, T Kawata, T Nakayama, and M Iwabuchi

Department of Botany, Faculty of Science, Kyoto University, Japan.

The structure and function of transcription factors of higher plants was studied by isolating cDNA clones encoding a wheat sequence-specific DNA binding protein. A hexameric nucleotide motif, ACGTCA, is located upstream from the TATA box of several plant histone genes. It has been suggested that this motif is essential for efficient transcription of the wheat histone H3 gene. A wheat nuclear protein, HBP-1 (histone DNA binding protein-1), which specifically binds to the hexameric motif, has previously been identified as a putative transcription factor. A cDNA clone encoding HBP-1 has been isolated on the basis of specific binding of HBP-1 to the hexameric motif. The deduced amino acid sequence indicates that HBP-1 contains the leucine zipper motif, which represents a characteristic property of several eukaryotic transcription factors.


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