Christos A. Panagiotidis, Shu-Ching Huang , Evangelos S. Canellakis
{"title":"大肠杆菌多胺生物合成的翻译后和转录调控","authors":"Christos A. Panagiotidis, Shu-Ching Huang , Evangelos S. Canellakis","doi":"10.1016/0020-711X(94)90070-1","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Ornithine and arginine decarboxylases (ODC and ADC) of <em>Escherichia coli</em> are inhibited post-translationally by antizyme and ribosomal proteins S20 and L34.</p></span></li><li><span>2.</span><span><p>2. The inhibition of either enzyme is relieved when excess of the other decarboxylase is added.</p></span></li><li><span>3.</span><span><p>3. Using this approach, <em>in vitro</em> as well as <em>in vivo</em>, we demonstrate that the extent of the post-translational inhibition of ODC and ADC in <em>E. coli</em> is at least 65 and 50%, respectively.</p></span></li><li><span>4.</span><span><p>4. The inhibited enzyme levels increase even further upon exposure of cells to polyamines.</p></span></li><li><span>5.</span><span><p>5. The post-translational mode of regulation can counteract a 4-fold increase of ODC protein in the cell.</p></span></li><li><span>6.</span><span><p>6. The negative transcriptional regulation of ODC and ADC expression by polyamines is mediated by transcription factors and not by direct polyamine effects on the promoters of their genes.</p></span></li><li><span>7.</span><span><p>7. Three proteins interacting with the ODC promoter region were found by southwestern blot analysis.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 8","pages":"Pages 991-1001"},"PeriodicalIF":0.0000,"publicationDate":"1994-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90070-1","citationCount":"14","resultStr":"{\"title\":\"Post-translational and transcriptional regulation of polyamine biosynthesis in Escherichia coli\",\"authors\":\"Christos A. Panagiotidis, Shu-Ching Huang , Evangelos S. Canellakis\",\"doi\":\"10.1016/0020-711X(94)90070-1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. Ornithine and arginine decarboxylases (ODC and ADC) of <em>Escherichia coli</em> are inhibited post-translationally by antizyme and ribosomal proteins S20 and L34.</p></span></li><li><span>2.</span><span><p>2. The inhibition of either enzyme is relieved when excess of the other decarboxylase is added.</p></span></li><li><span>3.</span><span><p>3. Using this approach, <em>in vitro</em> as well as <em>in vivo</em>, we demonstrate that the extent of the post-translational inhibition of ODC and ADC in <em>E. coli</em> is at least 65 and 50%, respectively.</p></span></li><li><span>4.</span><span><p>4. The inhibited enzyme levels increase even further upon exposure of cells to polyamines.</p></span></li><li><span>5.</span><span><p>5. The post-translational mode of regulation can counteract a 4-fold increase of ODC protein in the cell.</p></span></li><li><span>6.</span><span><p>6. The negative transcriptional regulation of ODC and ADC expression by polyamines is mediated by transcription factors and not by direct polyamine effects on the promoters of their genes.</p></span></li><li><span>7.</span><span><p>7. Three proteins interacting with the ODC promoter region were found by southwestern blot analysis.</p></span></li></ul></div>\",\"PeriodicalId\":13733,\"journal\":{\"name\":\"International Journal of Biochemistry\",\"volume\":\"26 8\",\"pages\":\"Pages 991-1001\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0020-711X(94)90070-1\",\"citationCount\":\"14\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International Journal of Biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0020711X94900701\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0020711X94900701","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Post-translational and transcriptional regulation of polyamine biosynthesis in Escherichia coli
1.
1. Ornithine and arginine decarboxylases (ODC and ADC) of Escherichia coli are inhibited post-translationally by antizyme and ribosomal proteins S20 and L34.
2.
2. The inhibition of either enzyme is relieved when excess of the other decarboxylase is added.
3.
3. Using this approach, in vitro as well as in vivo, we demonstrate that the extent of the post-translational inhibition of ODC and ADC in E. coli is at least 65 and 50%, respectively.
4.
4. The inhibited enzyme levels increase even further upon exposure of cells to polyamines.
5.
5. The post-translational mode of regulation can counteract a 4-fold increase of ODC protein in the cell.
6.
6. The negative transcriptional regulation of ODC and ADC expression by polyamines is mediated by transcription factors and not by direct polyamine effects on the promoters of their genes.
7.
7. Three proteins interacting with the ODC promoter region were found by southwestern blot analysis.
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