{"title":"小鼠Grg蛋白可能参与转录。","authors":"M Mallo, P M Lieberman, T Gridley","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The mouse Grg gene encodes a 197 amino acid nuclear protein homologous to the amino-terminal domain of the product of the groucho (gro) gene of the Drosophila Enhancer of split complex. Recent work has suggested that the gro protein functions as a transcriptional corepressor during Drosophila development. We therefore examined possible roles of the mouse Grg protein in DNA binding and in vitro transcription. No sequence-specific DNA binding activity was detected by polymerase chain reaction-DNA binding site selection nor was the glutamine-rich Grg protein capable of acting as an activation domain in an in vivo transactivation assay. However, depletion of Grg protein from HeLa nuclear extracts inhibited the in vitro transcription activity of the extracts. We suggest that Grg protein may interact with components of the basal transcription machinery.</p>","PeriodicalId":72545,"journal":{"name":"Cellular & molecular biology research","volume":"41 5","pages":"435-40"},"PeriodicalIF":0.0000,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Possible involvement of the mouse Grg protein in transcription.\",\"authors\":\"M Mallo, P M Lieberman, T Gridley\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The mouse Grg gene encodes a 197 amino acid nuclear protein homologous to the amino-terminal domain of the product of the groucho (gro) gene of the Drosophila Enhancer of split complex. Recent work has suggested that the gro protein functions as a transcriptional corepressor during Drosophila development. We therefore examined possible roles of the mouse Grg protein in DNA binding and in vitro transcription. No sequence-specific DNA binding activity was detected by polymerase chain reaction-DNA binding site selection nor was the glutamine-rich Grg protein capable of acting as an activation domain in an in vivo transactivation assay. However, depletion of Grg protein from HeLa nuclear extracts inhibited the in vitro transcription activity of the extracts. We suggest that Grg protein may interact with components of the basal transcription machinery.</p>\",\"PeriodicalId\":72545,\"journal\":{\"name\":\"Cellular & molecular biology research\",\"volume\":\"41 5\",\"pages\":\"435-40\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1995-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Cellular & molecular biology research\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Cellular & molecular biology research","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
小鼠Grg基因编码一个197个氨基酸的核蛋白,与果蝇分裂复合体增强子(Drosophila Enhancer of split complex)的grocho (gro)基因产物的氨基末端结构域同源。最近的研究表明,在果蝇发育过程中,gro蛋白作为一种转录辅抑制因子发挥作用。因此,我们研究了小鼠Grg蛋白在DNA结合和体外转录中的可能作用。聚合酶链反应-DNA结合位点选择没有检测到序列特异性DNA结合活性,富含谷氨酰胺的Grg蛋白也不能在体内转激活试验中作为激活域。然而,从HeLa核提取物中去除Grg蛋白会抑制提取物的体外转录活性。我们认为Grg蛋白可能与基础转录机制的组分相互作用。
Possible involvement of the mouse Grg protein in transcription.
The mouse Grg gene encodes a 197 amino acid nuclear protein homologous to the amino-terminal domain of the product of the groucho (gro) gene of the Drosophila Enhancer of split complex. Recent work has suggested that the gro protein functions as a transcriptional corepressor during Drosophila development. We therefore examined possible roles of the mouse Grg protein in DNA binding and in vitro transcription. No sequence-specific DNA binding activity was detected by polymerase chain reaction-DNA binding site selection nor was the glutamine-rich Grg protein capable of acting as an activation domain in an in vivo transactivation assay. However, depletion of Grg protein from HeLa nuclear extracts inhibited the in vitro transcription activity of the extracts. We suggest that Grg protein may interact with components of the basal transcription machinery.