A tomato genomic clone has been identified which encodes histone H1. The deduced polypeptide is 287 amino acids in length, and exhibits the tripartite organization typical of histones H1. The central globular domain is highly similar to those regions from other H1 molecules, and the carboxyl-terminal domain contains a repeating hexapeptide motif, variants of which are conserved among H1 molecules. RNA gel blotting revealed that histone H1 mRNA is expressed at higher levels in organs which contain meristematic tissue and/or which have a high proportion of actively cycling cells. DNA gel blotting and dot-blot hybridization studies revealed that histone H1 in tomato is encoded by a small gene family. By employing the polymerase chain reaction on genomic DNA and on cDNA, it was determined that the gene is interrupted by an intron. The location and approximate length of the intron are conserved in both the tomato and Arubidopsis genes, with the intron separating the 'nose' region (encoded by exon 1) from the central globular domain (exon 2). The promoter region was found to contain several conserved sequence motifs which likely participate in the regulation of the gene.In most eukaryotic cells, the most elementary level of chromatin packaging is accomplished by the interaction of two molecules of each of the core histones H2A, H2B, H3 and H4 with 146-bp of duplex DNA to yield the core particle of the nucleosome. Adjacent core particles are connected by a linker DNA region of approximately 40-60 bp and, on average, there exists one molecule of histone Hlhucleosome. While the sequences of the core histones are well conserved between widely divergent species, histone H1 molecules exhibit striking sequence divergence. Despite this divergence, histone H1 molecules have maintained three distinct regions. These consist of an amino-terminal 'nose', a conserved central globular domain and a positively charged carboxy-terminal tail. One role of histone H1 is to act at a second level of the hierarchy of chromatin packaging to direct the formation and maintenance of the 30-nm chromatin fiber. It is generally thought that the positively charged lysine residues, found predominantly in the tail region, neutralize the negative phosphates of linker DNA to permit compaction of the chromatin fiber. Several lines of evidence suggest that the conserved central globular domain is responsible for sealing the points of entry and exit of DNA from the core particle [7]. In the central globular domain of histone H1 molecules from both plants and animals, there are many conserved resi-