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Mol Cell Biol, May 1998, p. 2712-2720, Vol. 18, No. 5
Department of Zoology, University of British
Columbia, Vancouver, British Columbia, Canada V6T 1Z4
Received 30 July 1997/Returned for modification 12 September
1997/Accepted 28 January 1998
The Polycomb group proteins are transcriptional repressors that are
thought to act through multimeric nuclear complexes. We show that ph
and Psc coprecipitate with Pc from nuclear extracts. We have analyzed
the domains required for the association of Psc with ph and Pc by using
the yeast two-hybrid system and an in vitro protein-binding assay. Psc
and ph interact through regions of sequence conservation with mammalian
homologs, i.e., the H1 domain of ph (amino acids 1297 to 1418) and the
helix-turn-helix-containing region of Psc (amino acids 336 to 473). Psc
contacts Pc primarily at the helix-turn-helix-containing region of Psc
(amino acids 336 to 473), but also at the ring finger (amino acids 250 to 335). The Pc chromobox is not required for this interaction. We
discuss the implication of these results for the nature of the
complexes formed by Polycomb group proteins.
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
The Drosophila Polycomb Group Protein
Psc Contacts ph and Pc through Specific Conserved Domains
*
Corresponding author. Mailing address: Department of
Zoology, University of British Columbia, 6270 University Blvd.,
Vancouver, B.C., Canada V6T 1Z4. Phone: (604) 822-4456. Fax: (604)
822-2416. E-mail: brock{at}zoology.ubc.ca.
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