果蝇多梳蛋白组蛋白Psc通过特定的保守结构域与ph和Pc相互作用。
The Drosophila polycomb group protein Psc contacts ph and Pc through specific conserved domains.
作者信息
Kyba M, Brock H W
机构信息
Department of Zoology, University of British Columbia, Vancouver, Canada.
出版信息
Mol Cell Biol. 1998 May;18(5):2712-20. doi: 10.1128/MCB.18.5.2712.
Abstract
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.
摘要
多梳蛋白家族是一类转录抑制因子，被认为通过多聚体核复合物发挥作用。我们发现，在核提取物中，ph和Psc能与Pc共沉淀。我们利用酵母双杂交系统和体外蛋白结合试验，分析了Psc与ph和Pc结合所需的结构域。Psc和ph通过与哺乳动物同源物的序列保守区域相互作用，即ph的H1结构域（氨基酸1297至1418）和Psc的含螺旋-转角-螺旋区域（氨基酸336至473）。Psc主要在Psc的含螺旋-转角-螺旋区域（氨基酸336至473）与Pc接触，但也在其环指结构域（氨基酸250至335）与之接触。这种相互作用不需要Pc的染色质盒结构域。我们讨论了这些结果对多梳蛋白家族形成的复合物性质的影响。
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