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Nucleic Acids Research, 1992, Vol. 20, No. 22 6067-6074
© 1992

MOLECULAR BIOLOGY

Heterochromatin protein 1, a known suppressor of position-effect variegation, is highly conserved in Drosophila

Robert F. Clark and Sarah C.R. Elgin

Department of Biology, Box 1137, Washington University St Louis, MO 63130, USA

Received June 17, 1992. Revised October 19, 1992. Accepted October 19, 1992.

The Su(var)205 gene of Drosophila melanogaster encodes heterochromatin protein 1 (HP1), a protein located preferentially within ß-heterochromatin. Mutation of this gene has been associated with dominant suppression of position-effect variegation. We have cloned and sequenced the gene encoding HP1 from Drosophila virilis, a distantly related species. Comparison of the predicted amino acid sequence with Drosophila melanogaster HP1 shows two regions of strong homology, one near the N-terminus (57/61 amino acids identical) and the other near the C-terminus (62/68 amino acids identical) of the protein. Little homology is seen in the 5' and 3' untranslated portions of the gene, as well as in the intronic sequences, although intron/exon boundaries are generally conserved. A comparison of the deduced amino acid sequences of HP1-like proteins from other species shows that the cores of the N-terminal and C-terminal domains have been conserved from insects to mammals. The high degree of conservation suggests that these N- and C-terminal domains could interact with other macromolecules in the formation of the condensed structure of heterochromatin.


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