Abstract
The first H1 histone from a plant, Zea mays, has been characterized and partially sequenced. The maize H1 molecule shares many sequence features with rabbit and sea urchin H1 and chicken H5. The central hydrophobic region of the protein exhibits sequence microheterogeneity, indicating the presence of multiple H1 proteins in maize. The cause of the genetically controlled electrophoretic variation in the major H1 subfraction of maize has been localized to the carboxy-terminal region of the molecule.
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