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Vol. 12, Issue 6, 1671-1685, June 2001
and
*School of Biological Sciences, University of Kentucky, Lexington,
Kentucky 40506-0225; and Heterochromatin protein 1 (HP1) is a conserved component of the
highly compact chromatin of higher eukaryotic centromeres and
telomeres. Cytogenetic experiments in Drosophila have
shown that HP1 localization into this chromatin is perturbed in mutants for the origin recognition complex (ORC) 2 subunit. ORC has a multisubunit DNA-binding activity that binds origins of DNA replication where it is required for origin firing. The DNA-binding activity of ORC
is also used in the recruitment of the Sir1 protein to silence
nucleation sites flanking silent copies of the mating-type genes in
Saccharomyces cerevisiae. A fraction of HP1 in the
maternally loaded cytoplasm of the early Drosophila
embryo is associated with a multiprotein complex containing
Drosophila melanogaster ORC subunits. This
complex appears to be poised to function in heterochromatin assembly
later in embryonic development. Here we report the identification of a
novel component of this complex, the HP1/ORC-associated protein. This
protein contains similarity to DNA sequence-specific HMG proteins and
is shown to bind specific satellite sequences and the
telomere-associated sequence in vitro. The protein is shown to have
heterochromatic localization in both diploid interphase and mitotic
chromosomes and polytene chromosomes. Moreover, the gene encoding
HP1/ORC-associated protein was found to display reciprocal
dose-dependent variegation modifier phenotypes, similar to those for
mutants in HP1 and the ORC 2 subunit.
Department of Biological
Sciences, McGill University, Montreal, Quebec H3A 1B1, Canada
Corresponding author. E-mail address:
rkellum{at}pop.uky.edu.
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