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Nucleic Acids Research, 1991, Vol. 19, No. 7 1491-1496
© 1991

MOLECULAR BIOLOGY

Nucleotide sequence and expression of a maize H1 histone cDNA

P. Razafimahatratra, N. Chaubet, G. Philipps and C. Gigot*

Institut de Biologie Moléculaire des Plantes du CNRS, Universé Louis Pasteur 12 rue du Général Zimmer, 67084 Strasbourg Cédex, France

* To whom correspondence should be addressed

Received January 8, 1991. Revised March 1, 1991. Accepted March 1, 1991.

The first complete amino acid sequence of a H1 histone of a monocotyledonous plant was deduced from a cDNA isolated from a maize library. The encoded H1 protein is 245 amino acid-long and shows the classical tripartite organization of this class of histones. The central globular region of 76 residues shows 60% sequence homology with H1 proteins from dicots but only 20% with the animal H1 proteins. However, several of the amino acids considered as being important in the structure of the nucleosome are conserved between this protein and its animal counterparts. The N-terminal region contains an equal number of acidic and basic residues which appears as a general feature of plant H1 proteins. The 124 residue long and highly basic C-termlnal region contains a 7-fold repeated element KA/PKXA/PAKA/PK. Southern-blot hybridization showed that the H1 protein is encoded by a small multigene family. Highly homologous H1 gene families were also detected in the genomes of several more or less closely related plant species. The general expression pattern of these genes was not significantly different from that of the genes encoding the core-histones neither during germination nor in the different tissues of adult maize.


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