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Nucleic Acids Research, 1994, Vol. 22, No. 2 180-186
© 1994

MOLECULAR BIOLOGY

Independent evolutionary origin of histone H3.3-like variants of animals and Tetrahymena

Thomas H. Thatcher+, Jennifer MacGaffey, Josephine Bowen, Stuart Horowitz§, Donald L. Shapiro and Martin A. Gorovsky*

Department of Biology, University of Rochester Rochester, NY 14627, USA

*To whom correspondence should be addressed

Received October 26, 1993. Accepted December 7, 1993.

All three genes encoding histone H3 proteins were cloned and sequenced from Tetrahymena thermophlla. Two of these genes encode a major H3 protein Identical to that of T.pyriformis and 87% Identical to the major H3 of vertebrates. The third gene encodes hv2, a quantitatively minor replication independent (replacement) variant. The sequence of hv2 is only 85% Identical to the animal replacement variant H3.3 and is the most divergent H3 replacement variant described. Phylogenetlc analysis of 73 H3 protein sequences suggests that hv2, H3.3, and the plant replacement variant H3.III evolved Independently, and that H3.3 Is not the ancestral H3 gene, as was previously suggested (Wells, D., Bains, W., and Kedes, L. 1986. J. Mol. Evol., 23: 224–241). These results suggest It Is the replication Independence and not the particular protein sequence that Is important in the function of H3 replacement variants.

+Present address: School of Medicine and Dentistry, University of Rochester, 601 Elmwood Avenue, PO Box 363, Rochester, NY 14642.

§Present address: CardioPulirtonary Research Institute, Suite 503, Winthrop University Hospital, 222 Station Plaza North, Mineola, NY 11501, USA.


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