{"title":"小鼠乳腺肿瘤病毒和其他逆转录病毒的翻译移码抑制。","authors":"J Majors","doi":"10.1159/000468768","DOIUrl":null,"url":null,"abstract":"<p><p>Retroviruses, related retroposons, and several RNA viruses use translational frameshifting in the expression of their polymerase genes. We use retroviruses, particularly mouse mammary tumor virus, to illustrate the model which reflects our current understanding of these site-specific frameshifting events. The model has two components, a shifty sequence that facilitates ribosome slippage, and a second signal, either RNA secondary structure or an unfilled ribosomal A site, that stalls the ribosome and increases the probability of slippage at the shifty site.</p>","PeriodicalId":11933,"journal":{"name":"Enzyme","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000468768","citationCount":"2","resultStr":"{\"title\":\"Translational frameshift suppression in mouse mammary tumor virus and other retroviruses.\",\"authors\":\"J Majors\",\"doi\":\"10.1159/000468768\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Retroviruses, related retroposons, and several RNA viruses use translational frameshifting in the expression of their polymerase genes. We use retroviruses, particularly mouse mammary tumor virus, to illustrate the model which reflects our current understanding of these site-specific frameshifting events. The model has two components, a shifty sequence that facilitates ribosome slippage, and a second signal, either RNA secondary structure or an unfilled ribosomal A site, that stalls the ribosome and increases the probability of slippage at the shifty site.</p>\",\"PeriodicalId\":11933,\"journal\":{\"name\":\"Enzyme\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1990-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1159/000468768\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Enzyme\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1159/000468768\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Enzyme","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000468768","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Translational frameshift suppression in mouse mammary tumor virus and other retroviruses.
Retroviruses, related retroposons, and several RNA viruses use translational frameshifting in the expression of their polymerase genes. We use retroviruses, particularly mouse mammary tumor virus, to illustrate the model which reflects our current understanding of these site-specific frameshifting events. The model has two components, a shifty sequence that facilitates ribosome slippage, and a second signal, either RNA secondary structure or an unfilled ribosomal A site, that stalls the ribosome and increases the probability of slippage at the shifty site.