{"title":"Posttranscriptional Regulation by the HIV-1 Rev Protein","authors":"Bryan R. Cullen","doi":"10.1006/smvy.1997.0135","DOIUrl":"10.1006/smvy.1997.0135","url":null,"abstract":"<div><p>Human Immunodeficiency Virus Type 1 (HIV-1) encodes a range of mRNA species derived by partial or complete splicing of a single initial RNA transcript. The nuclear export of the incompletely spliced class of HIV-1 RNAs, which encode critical viral structural proteins, is dependent on the Rev post-transcriptional regulatory protein, a viral RNA binding factor that is expressed early in the HIV-1 replication cycle. Rev contains a potent nuclear export signal that mediates the nucleocytoplasmic transport of bound RNAs subsequent to an interaction with components of the nuclear pore. It has now become evident that the nuclear export pathway utilized by HIV-1 Rev is also critical for the nuclear export of a range of cellular proteins and RNAs.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 4","pages":"Pages 327-334"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1997.0135","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51141959","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Posttranscriptional Regulation of Gene Expression in Hepadnaviruses","authors":"T.S. Benedict Yen","doi":"10.1006/smvy.1997.0134","DOIUrl":"10.1006/smvy.1997.0134","url":null,"abstract":"<div><p>The hepadnaviruses utilize multiple nested promoters on the same DNA strand to transcribe several mRNA species, all of which terminate at the same polyadenylation site. While most studies of hepadnaviral gene expression have concentrated on transcriptional initiation, it has become clear that there exist viral<em>cis</em>-elements that are important in posttranscriptional events. This review will describe recent data on transcriptional elongation, transcriptional termination, and RNA export in hepadnaviruses and compare them with the corresponding processes in the distantly related retroviruses.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 4","pages":"Pages 319-326"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1997.0134","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51141886","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Posttranscriptional Regulation in Herpes Simplex Virus","authors":"Anne Phelan , J.Barklie Clements","doi":"10.1006/smvy.1997.0133","DOIUrl":"10.1006/smvy.1997.0133","url":null,"abstract":"<div><p>The essential herpes simplex virus type 1 (HSV-1) immediate-early protein IE63 (ICP27) is an RNA binding protein which, at the posttranscriptional level, interacts with cellular splicing small nuclear ribonucleoprotein particles (snRNPs) and inhibits RNA splicing, promotes RNA 3′ processing, and prevents the nucleocytoplasmic transport of intron-containing mRNAs. IE63 is the only HSV IE protein with homologs not only among other α herpesviruses, but also throughout the herpesviridae family. Recent evidence shows that IE63 is a nucleocytoplasmic shuttle protein able to travel from snRNP- and RNA-rich nuclear foci to the cytoplasm. This property suggests that IE63 may facilitate the nuclear export of virus mRNAs, perhaps selectively, of HSV-1 transcripts, from virus genes which lack introns. Posttranscriptional effects of other HSV-1 functions are discussed.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 4","pages":"Pages 309-318"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1997.0133","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51141648","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Multiple Levels of Posttranscriptional Regulation of Influenza Virus Gene Expression","authors":"Juan Ortı́n","doi":"10.1006/smvy.1997.0136","DOIUrl":"10.1006/smvy.1997.0136","url":null,"abstract":"<div><p>The genome of Influenza viruses consists of a set of single-stranded, negative-polarity ribonucleoproteins. Each one is replicated and transcribed as an independent unit in the nucleus of the infected cell. This property allows the existence of both nuclear and cytoplasmic regulatory steps in the control of viral gene expression at the posttranscriptional level. The regulation of mRNA splicing and nucleocytoplasmic mRNA transport and the preferential translation of viral mRNAs in the infected cell are discussed, stressing the possible role of NS1 protein in these processes.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 4","pages":"Pages 335-342"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1997.0136","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51142038","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Joseph Curran , Patrizia Latorre, Daniel Kolakofsky
{"title":"Translational Gymnastics on the Sendai Virus P/C mRNA","authors":"Joseph Curran , Patrizia Latorre, Daniel Kolakofsky","doi":"10.1006/smvy.1997.0138","DOIUrl":"10.1006/smvy.1997.0138","url":null,"abstract":"<div><p>The Sendai virus (SeV) P/C mRNA expresses eight different polypeptide chains using a combination of ribosomal choice and cotranscriptional editing (an internal open reading frame (ORF) is accessed by the addition of a single G residue after a short run of Gs at position 1053 on the mRNA). The longest ORF within the mRNA starts at ATG104 (the second initiation site) and encodes the 568-aa P protein, an essential viral structural protein which serves both as a cofactor for the RNA-dependant RNA polymerase (L protein) and as a part of the assembly complex. The first (ACG81), third (ATG114), fourth (ATG183) and fifth (ATG201) initiation sites are used to express a C-terminal nested set of polypeptides which are in the +1 ORF relative to P, namely C′, C, Y1, and Y2, respectively (collectively named the C proteins). Leaky scanning accounts for translational initiation at the first three start sites (a non-ATG followed by ATGs in progressively stronger contexts). Consistent with this, changing the C′ ACG to an ATG (GCCATG81G; ATG81/C′) ablates all expression from the downstream ATG104/P and ATG114/C initiation codons, whereas initiation from ATG183/Y1 and ATG201/Y2 remains normal in this background. Initiation from ATG183/Y1/ ATG201/Y2 probably takes place by discontinuous scanning via a ribosomal shunt. Scanning complexes appear to assemble at the 5′ cap and then scan the first ≈30 nt of the 5′ UTR before being translocated to an acceptor site close to the Y initiation codons. No specific 5′ UTR or donor site sequence elements are required, and translation of the Y proteins continues even when their start codons are changed to ACG.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 4","pages":"Pages 351-357"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1997.0138","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51142258","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cis-Acting Negative RNA Elements on Papillomavirus Late mRNAs","authors":"Stefan Schwartz","doi":"10.1006/smvy.1997.0131","DOIUrl":"10.1006/smvy.1997.0131","url":null,"abstract":"<div><p>Papillomaviruses comprise a large number of related small DNA tumor viruses with tropism for squamous epithelial cells. The papillomavirus replication cycle is strictly linked to the differentiation stages of the infected epithelial cells, and the expression of L1 and L2 capsid proteins from the viral late genes is primarily detected in the superficial layers of terminally differentiated cells. Expression of the L1 and L2 genes is blocked in nonterminally differentiated cells and the production of progeny virus is delayed until the infected cell reaches the upper strata of the squamous epithelium. This property presumably aids the papillomavirus to evade the immune surveillance of the host and allows establishment of persistent infections. Late gene expression levels are determined in part by regulatory RNA sequences on the papillomavirus mRNAs. This review focuses primarily on negative<em>cis</em>-acting elements on late papillomavirus mRNAs and their candidate<em>trans</em>-acting factors. Identification and characterization of these components will contribute to our understanding of the regulated expression of papillomaviruses in mammalian cells.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 4","pages":"Pages 291-300"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1997.0131","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51141540","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Regulated RNA Processing and RNA Transport during Adenovirus Infection","authors":"Keith N. Leppard","doi":"10.1006/smvy.1997.0132","DOIUrl":"10.1006/smvy.1997.0132","url":null,"abstract":"<div><p>Adenovirus (Ad) gene expression involves regulation both of RNA processing and RNA transport. The major late transcription unit (MLTU) in particular requires complex differential splicing and polyadenylation to produce its full array of mRNA and the pattern of processing changes as infection proceeds. Many MLTU mRNAs cannot reach the cytoplasm effectively without viral functions, probably because they are recognized by host nuclear retention mechanisms. Infection produces changes to the activity of cellular splicing factors and polyadenylation factors so altering the relative recognition of competing RNA processing sites as infection proceeds. In addition, three Ad proteins, E1B 55K, E4 Orf3, and E4 Orf6 are involved in posttranscriptional regulation. These directly or indirectly alter the pattern of MLTU splicing, facilitate late RNA export, and alter the distribution of cellular antigens within the nucleus.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 4","pages":"Pages 301-307"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1997.0132","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51141634","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"mRNA 3′ End Formation by Vaccinia Virus: Mechanism of Action of a Heterodimeric Poly(A) Polymerase","authors":"Paul D. Gershon","doi":"10.1006/smvy.1997.0137","DOIUrl":"10.1006/smvy.1997.0137","url":null,"abstract":"<div><p>Historically, vaccinia viral enzymes have provided fundamental insights into general enzymological processes. Reasons for this include their amenity to genetic approaches, the relative ease with which they can be purified in adequate quantities, their genetic location within a relatively small, intronless, completely sequenced genome, and the recognizable sequence similarity often observed with corresponding cellular enzymes. Mechanisms by which the ubiquitous poly(A) tail is added to mRNA 3′ ends are not fully characterized in any organism. Concurrently with the characterization of the metazoan, yeast, and<em>Escherichia coli</em>poly(A) polymerases, some recent biochemical and crystallographic studies of the vaccinia enzyme have provided glimpses of how a heterodimeric poly(A) polymerase might elongate the poly(A) tail.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 4","pages":"Pages 343-350"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1997.0137","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51142094","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Antoine A.F. de Vries, Marian C. Horzinek, Peter J.M. Rottier, Raoul J. de Groot
{"title":"The Genome Organization of the Nidovirales: Similarities and Differences between Arteri-, Toro-, and Coronaviruses","authors":"Antoine A.F. de Vries, Marian C. Horzinek, Peter J.M. Rottier, Raoul J. de Groot","doi":"10.1006/smvy.1997.0104","DOIUrl":"10.1006/smvy.1997.0104","url":null,"abstract":"<div><p>Viruses in the families Arteriviridae and Coronaviridae have enveloped virions which contain nonsegmented, positive-stranded RNA, but the constituent genera differ markedly in genetic complexity and virion structure. Nevertheless, there are striking resemblances among the viruses in the organization and expression of their genomes, and sequence conservation among the polymerase polyproteins strongly suggests that they have a common ancestry. On this basis, the International Committee on Taxonomy of Viruses recently established a new order, Nidovirales, to contain the two families. Here, the common traits and distinguishing features of the Nidovirales are reviewed.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 1","pages":"Pages 33-47"},"PeriodicalIF":0.0,"publicationDate":"1997-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1997.0104","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37832376","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Polyprotein Processing as a Strategy for Gene Expression in RNA Viruses","authors":"Valerie E. Spall, M. Shanks, G.P. Lomonossoff","doi":"10.1006/smvy.1997.0102","DOIUrl":"10.1006/smvy.1997.0102","url":null,"abstract":"<div><p>RNA viruses in many families and genera express their genomes in ways which involve the synthesis and subsequent cleavage of precursor polyproteins. This strategem allows the activation of subsets of proteins with different biochemical functions from the same precursor protein. Although the virus-encoded enzymes responsible for processing the polyproteins are structurally diverse, they are all highly specific for their substrates. The resulting processing cascade is a tightly controlled process, which in several cases involves the action of protein cofactors to modulate the activity of the proteinase.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 1","pages":"Pages 15-23"},"PeriodicalIF":0.0,"publicationDate":"1997-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1997.0102","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51139683","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}