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Zeste Maintains Repression of Ubx Transgenes: Support for a New Model of Polycomb Repression.

DE2005835803

Publication Date	2005
Personal Author	Hur, M. W.; Laney, J. D.
Page Count	26
Abstract	During late embryogenesis, the expression domains of homeotic genes are maintained by two groups of ubiquitously expressed regulators: the Polycomb repressors and the Trithorax activators. It is not known how the activities of the two maintenance systems are initially targeted to the correct genes. Zeste and GAGA are sequence specific DNA binding proteins previously shown to be Trithorax group activators of the homeotic gene Ultrabithorax (Ubx). Here we demonstrate that Zeste and GAGA DNA binding sites at the proximal promoter are also required to maintain, but not to initiate, repression of Ubx. Further, the repression mediated by Zeste DNA binding site is abolished in zeste null embryos. These data imply that Zeste and probably GAGA mediate Polycomb repression. We present a model in which the dual transcriptional activities of Zeste and GAGA are an essential component of the mechanism that chooses which maintenance system is to be targeted to a given promoter.
Keywords	Regulators Genes Models Promoters Binding sites Embryogenesis Polycomb repressors Trithorax activators Zeste Homeotic genes Expression domains DNA binding proteins GAGA
Source Agency	Technical Information Center Oak Ridge Tennessee
Corporate Authors	Yonsei Univ., Seoul (Republic of Korea). Dept. of Civil Engineering.; Department of Energy, Washington, DC.; Yale Univ., New Haven, CT. Dept. of Molecular Cellular and Developmental; Kon-Kuk Univ., Department of Biology, Seoul (Korea).; Harvard Medical School, Boston, MA. Dept. of Biological Chemistry and
Supplemental Notes	Prepared in cooperation with Yale Univ., New Haven, CT. Dept. of Molecular Cellular and Developmental Biology., Kon-Kuk Univ., Department of Biology, Seoul (Korea). and Harvard Medical School, Boston, MA. Dept. of Biological Chemistry and Molecular Pharmacology. Sponsored by Department of Energy, Washington, DC.
Document Type	Technical Report
NTIS Issue Number	200519

Zeste Maintains Repression of Ubx Transgenes: Support for a New Model of Polycomb Repression.

Zeste Maintains Repression of Ubx Transgenes: Support for a New Model of Polycomb Repression.
DE2005835803

Publication Date	2005
Personal Author	Hur, M. W.; Laney, J. D.
Page Count	26
Abstract	During late embryogenesis, the expression domains of homeotic genes are maintained by two groups of ubiquitously expressed regulators: the Polycomb repressors and the Trithorax activators. It is not known how the activities of the two maintenance systems are initially targeted to the correct genes. Zeste and GAGA are sequence specific DNA binding proteins previously shown to be Trithorax group activators of the homeotic gene Ultrabithorax (Ubx). Here we demonstrate that Zeste and GAGA DNA binding sites at the proximal promoter are also required to maintain, but not to initiate, repression of Ubx. Further, the repression mediated by Zeste DNA binding site is abolished in zeste null embryos. These data imply that Zeste and probably GAGA mediate Polycomb repression. We present a model in which the dual transcriptional activities of Zeste and GAGA are an essential component of the mechanism that chooses which maintenance system is to be targeted to a given promoter.
Keywords	Regulators Genes Models Promoters Binding sites Embryogenesis Polycomb repressors Trithorax activators Zeste Homeotic genes Expression domains DNA binding proteins GAGA
Source Agency	Technical Information Center Oak Ridge Tennessee
Corporate Authors	Yonsei Univ., Seoul (Republic of Korea). Dept. of Civil Engineering.; Department of Energy, Washington, DC.; Yale Univ., New Haven, CT. Dept. of Molecular Cellular and Developmental; Kon-Kuk Univ., Department of Biology, Seoul (Korea).; Harvard Medical School, Boston, MA. Dept. of Biological Chemistry and
Supplemental Notes	Prepared in cooperation with Yale Univ., New Haven, CT. Dept. of Molecular Cellular and Developmental Biology., Kon-Kuk Univ., Department of Biology, Seoul (Korea). and Harvard Medical School, Boston, MA. Dept. of Biological Chemistry and Molecular Pharmacology. Sponsored by Department of Energy, Washington, DC.
Document Type	Technical Report
NTIS Issue Number	200519