The extra sex combs product contains WD40 repeats and its time of action implies a role distinct from other Polycomb group products

Simon, John; Bornemann, Douglas J.; Lunde, Karen; Schwartz, Christopher

doi:10.1016/0925-4773(95)00434-3

Cited by 61 publications

(70 citation statements)

References 75 publications

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“…Absence of the esc gene product during this short period results in homeotic transformations which are very similar to those of other PcG mutations. However, when the esc protein is missing during earlier or, most importantly, during later phases in development, no phenotypical defects are observed (39,40). This finding indicates a role for esc which is different from these other PcG genes.…”

Section: Discussioncontrasting

confidence: 36%

“…The predicted 535-aa-long protein is identical to the mouse eed protein (7) and we therefore name the novel human protein EED. The eed (for embryonic ectoderm development) gene (7,36) has been identified as being a vertebrate homolog of the Drosophila PcG gene esc (14,32,39). Within the 1,605-bp-long coding region, EED is 93% identical with eed at the nucleotide level.…”

Section: Resultsmentioning

confidence: 99%

“…esc is a PcG protein which also stands apart from other PcG proteins. PcG genes play a crucial role in the maintenance of homeotic gene activity during later phases of embryonic development, but for esc an earlier role has been proposed (14,32,39,40). First, the esc gene is expressed only during a limited, very early developmental phase of Drosophila development (39).…”

Section: Discussionmentioning

confidence: 99%

“…Here, we report the identification of the human EED protein, which interacts with Enx1/EZH2. EED is the human homolog of eed, a murine PcG gene (7,36) which has extensive homology with the Drosophila PcG gene extra sex combs (esc) (14,32,39). Whereas Enx1/ EZH2 and EED coimmunoprecipitate, they neither coimmunoprecipitate nor colocalize with other human PcG proteins, such as HPC2 and BMI1.…”

mentioning

confidence: 99%

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Characterization of Interactions between the Mammalian Polycomb-Group Proteins Enx1/EZH2 and EED Suggests the Existence of Different Mammalian Polycomb-Group Protein Complexes

Sewalt

Vlag

Gunster

et al. 1998

Molecular and Cellular Biology

211

198

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In Drosophila melanogaster, the Polycomb-group (PcG) and trithorax-group (trxG) genes have been identified as repressors and activators, respectively, of gene expression. Both groups of genes are required for the stable transmission of gene expression patterns to progeny cells throughout development. Several lines of evidence suggest a functional interaction between the PcG and trxG proteins. For example, genetic evidence indicates that the enhancer of zeste [E(z)] gene can be considered both a PcG and a trxG gene. To better understand the molecular interactions in which the E(z) protein is involved, we performed a two-hybrid screen with Enx1/EZH2, a mammalian homolog of E(z), as the target. We report the identification of the human EED protein, which interacts with Enx1/EZH2. EED is the human homolog of eed, a murine PcG gene which has extensive homology with the Drosophila PcG gene extra sex combs (esc). Enx1/EZH2 and EED coimmunoprecipitate, indicating that they also interact in vivo. However, Enx1/EZH2 and EED do not coimmunoprecipitate with other human PcG proteins, such as HPC2 and BMI1. Furthermore, unlike HPC2 and BMI1, which colocalize in nuclear domains of U-2 OS osteosarcoma cells, Enx1/EZH2 and EED do not colocalize with HPC2 or BMI1. Our findings indicate that Enx1/EZH2 and EED are members of a class of PcG proteins that is distinct from previously described human PcG proteins.In Drosophila melanogaster, the genes of the Polycomb group (PcG) and trithorax group (trxG) are part of a cellular memory system, which is responsible for the stable inheritance of gene activity. The PcG and trxG genes have been identified in Drosophila as repressors (PcG) (18,22,27,28,38) and activators (trxG) (20, 21), respectively, of homeotic gene activity. PcG and trxG genes were originally found in Drosophila, but mammalian homologs have also been identified and appear to function like their Drosophila homologs (reviewed in reference 37). It has been proposed that PcG proteins repress gene expression through the formation of multimeric protein complexes. We have recently shown that the human PcG proteins HPH1 and HPH2 coimmunoprecipitate, cofractionate, and colocalize in nuclear domains with the human PcG proteins BMI1 (2, 12, 33) and HPC2, a recently identified, novel human Polycomb protein (33,34). Furthermore, we have found that the human RING1 protein coimmunoprecipitates and colocalizes with HPC2 and other PcG proteins, indicating that RING1 is associated with, or is part of, the mammalian PcG complex (33, 35). These results indicate that mammalian PcG proteins form a multimeric protein complex.

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Section: Discussioncontrasting

confidence: 36%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Characterization of Interactions between the Mammalian Polycomb-Group Proteins Enx1/EZH2 and EED Suggests the Existence of Different Mammalian Polycomb-Group Protein Complexes

Sewalt

Vlag

Gunster

et al. 1998

Molecular and Cellular Biology

211

198

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“…Regulation of histone methylation by SET domain-containing methyltransferases via their interaction with other proteins has been demonstrated in yeast and mammalian systems [48,72,109]. In plants, the regulation of SET protein-mediated histone methylation through proteinprotein interactions is poorly understood.…”

Section: Regulation Of Set Protein Functions Through Protein-proteinmentioning

confidence: 99%

Plant SET domain-containing proteins: Structure, function and regulation

Wang

Chandrasekharan

et al. 2007

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expres

176

195

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Modification of the histone proteins that form the core around which chromosomal DNA is looped has profound epigenetic effects on the accessibility of the associated DNA for transcription, replication and repair. The SET domain is now recognized as generally having methyltransferase activity targeted to specific lysine residues of histone H3 or H4. There is considerable sequence conservation within the SET domain and within its flanking regions. Previous reviews have shown that SET proteins from Arabidopsis and maize fall into five classes according to their sequence and domain architectures. These classes generally reflect specificity for a particular substrate. SET proteins from rice were found to fall into similar groupings, strengthening the merit of the approach taken. Two additional classes, VI and VII, were established that include proteins with truncated/ interrupted SET domains. Diverse mechanisms are involved in shaping the function and regulation of SET proteins. These include protein-protein interactions through both intra-and inter-molecular associations that are important in plant developmental processes, such as flowering time control and embryogenesis. Alternative splicing that can result in the generation of two to several different transcript isoforms is now known to be widespread. An exciting and tantalizing question is whether, or how, this alternative splicing affects gene function. For example, it is conceivable that one isoform may debilitate methyltransferase function whereas the other may enhance it, providing an opportunity for differential regulation. The review concludes with the speculation that modulation of SET protein function is mediated by antisense or sense-antisense RNA.

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Mouse homolog of theDrosophila Pc-G geneesc exerts a dominant negative effect inDrosophila

Wang

Tie

Jane

et al. 2000

genesis

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The extra sex combs product contains WD40 repeats and its time of action implies a role distinct from other Polycomb group products

Cited by 61 publications

References 75 publications

Characterization of Interactions between the Mammalian Polycomb-Group Proteins Enx1/EZH2 and EED Suggests the Existence of Different Mammalian Polycomb-Group Protein Complexes

Characterization of Interactions between the Mammalian Polycomb-Group Proteins Enx1/EZH2 and EED Suggests the Existence of Different Mammalian Polycomb-Group Protein Complexes

Plant SET domain-containing proteins: Structure, function and regulation

Mouse homolog of theDrosophila Pc-G geneesc exerts a dominant negative effect inDrosophila

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