Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.7.48 (transcriptase)
9,479 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Upon infection of Chinese hamster ovary cells (CHO), vesicular stomatitis (VSV) virus synthesizes two membrane proteins (the VSV glycoprotein and the VSV matrix or membrane (M) protein) and three nonmembrane proteins (the VSV nucleocapsid, the viral transcriptase, and an NS protein). We have used the VSV-infected cell as a model system for the study of the site of synthesis of these membrane and nonmembrane proteins. We have isolated VSV mRNA from free polyribosomes, membrane-bound polyribosomes, and the postribosomal supernatant, and identified the individual species of VSV mRNA present in each fraction. The mRNA which encodes the VSV glycoprotein is found exclusively on membrane-bound polyribosomes, while the mRNAs which encode the VSV, M, N, and NS proteins are found in free polyribosomes, in the membrane fraction of the cell, and in the postribosomal supernatant. Our results suggest that the VSV glycoprotein is synthesized exclusively on membrane polyribosomes, while at least some of the M, N, and NS proteins are made on free polyribosomes.
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PMID:Site of synthesis of membrane and nonmembrane proteins of vesicular stomatitis virus. 16 63

The virion transcriptase (nucleosidetriphosphate: RNA nucleotidyltransferase, EC 2.7.7.6) of vesicular stomatitis virus was fully active when ribonucleoprotein cores from purified virions were added to cell-free protein synthesizing systems of eukaryotic origin. Synthesis of mRNA was linear for at least 3 hr and the newly synthesized viral mRNA was efficiently utilized for the synthesis of viral proteins N (nucleoprotein), NS, and M (matrix); small amounts of a putative G (glycoprotein protein precursor and several unidentified polypeptides were regularly synthesized. The ratio of the various newly synthesized viral proteins was identical after different periods of coupled mRNA and protein synthesis. Identical proteins were obtained when the cell-free protein synthesizing systems were programmed with purified VSV mRNA synthesized in vitro. No detectable L protein was synthesized, even though transcripts complementary to the complete viral genome were detectable in the mRNA preparation by hybridization.
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PMID:Coupled in vitro transcription and translation of vesicular stomatitis virus messenger RNA. 17 Jun 4

The family Rhabdoviridae comprises approximately 75 viruses infecting vertebrates, invertebrates and plants. The main characteristics of the member viruses are: (i) the viruses infecting vertebrates and invertebrates are bullet-shaped and the viruses infecting plants are usually bacilliform; (ii) the viruses have particle lengths varying from 130 to 380 nm and widths varying from 60 to 95 nm; (iii) the viruses possess unit-membrane envelopes from which protrude spikes 5 to 10 nm long; (iv) the viruses have precisely coiled helical nuecleocapsids with a diameter of approx. 50 nm; (v) most of the viruses which have been studied contain 5 proteins; the prototype, vesicular stomatitis virus, contains proteins designated L (large), G (glycoprotein), N (nucleoprotein), NS (nonstructural) and M (matrix); N or NS is phosphorylated in most members which have been studied; (vi) the viruses contain single-stranded RNA which is transcribed into several messenger RNA species with sizes corresponding to the structural proteins; (vii) the nucleocapsid contains the RNA-dependent RNA polymerase and is infectious; and (viii) many of the viruses produce morphologically distinct defective-interfering (T) particles.
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PMID:Rhabdoviridae. Report of the Rhabdovirus Study Group, International Committee on Taxonomy of Viruses. 50 Mar 29

The association of an RNA-dependent RNA polymerase activity with virions of pike fry rhabdovirus has been demonstrated by both in vitro and in vivo studies. The temperature optimum for the in vitro assay is around 20 C, although enzyme activity can be observed at 4 C. Preparations of pike fry virus possess a glycoprotein, a membrane protein, a nucleoprotein, an L protein, and a phosphoprotein, as well as an RNA of about 3.8 times 10-6 mol wt. A protein kinase activity has been found associated with virus preparations. In vitro RNA product analyses indicate that the virus-associated enzyme functions principally as a transcriptase synthesizing viral-complementary, heteropolymeric RNA.
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PMID:RNA polymerase associated with virions of pike fry rhabdovirus. 116 3

During persistent infection of mouse L cells with strain Armstrong lymphocytic choriomeningitis virus, the latter undergoes characteristic changes, including loss of mouse pathogenicity and failure to form plaques on cultivated cells. We call this virus L(Arm) and have analyzed transcription and translation of its S-RNA, which codes for the viral nucleoprotein (NP) and the glycoprotein precursor (GP-C). In L(Arm) virus-infected L cells, S-RNA and genomic-sized viral complementary S-RNA (VC-S-RNA) were detected and, in addition, considerable quantities of shortened molecules of either species. The cells' content of NP was high, but they contained little GP-C; instead, a viral glycoprotein with MW 65,000 was present. We propose a hypothesis in which it is assumed that along the VC-S-RNA there is more than one recognition site for the viral RNA-dependent RNA polymerase, which leads to the generation of truncated forms of S-RNA, VC-S-RNA, and mRNA for GP-C; this, in turn, results in relative overproduction of NP and relative underproduction of GP-C as well as the emergence of a new form of viral glycoprotein.
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PMID:Mode of replication of lymphocytic choriomeningitis virus in persistently infected cultivated mouse L cells. 169 11

The vesicular stomatitis virus thermolabile mutant tl17 contains multiple lesions. The RNA-dependent RNA polymerase is temperature sensitive during primary transcription. The glycoprotein develops Endo H sensitivity more slowly at the nonpermissive temperature. Maturation or incorporation of the glycoprotein into progeny virions is also reduced. When virions of tl17 made at the permissive temperature are incubated in buffered medium at 39 degrees, their glycoprotein is cleaved, resulting in a product that resembles soluble glycoprotein. Compared to another glycoprotein mutant, ts 045, the glycoprotein of tl17 is only partially degraded to soluble G intracellularly and is more thermolabile. These properties of tl17 make it potentially useful for studies on glycoprotein synthesis, processing, and transport as well as for studies on pseudotype formation and viral maturation.
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PMID:Multiple thermolabile and temperature-sensitive lesions in mutant tl17 of vesicular stomatitis virus. 247 64

The infection and coding strategies of three groups of negative-stranded RNA viruses (arena viruses, phleboviruses, and nairoviruses) that include the etiologic agents of hemorrhagic disease in humans have been studied. Arenaviruses have two viral RNA species. The smaller RNA species (S) codes for the viral nucleoprotein (N protein) and for the viral glycoprotein species (G1 and G2, which are derived from a precursor glycoprotein, GPC). The S RNA has an ambisense arrangement. The proteins are translated from subgenomic mRNA species (viz., N protein from a viral-complementary mRNA and glycoprotein from a viral-sense mRNA). The larger arenavirus RNA species (L) is presumed to code for the viral transcriptase/replicase. Phleboviruses and nairoviruses are members of the Bunyaviridae. They both have three species of viral RNA. Other than the sizes of the viral proteins and the viral RNA species, virtually nothing is known about the coding strategy of nairoviruses. Phleboviruses have an ambisense coding arrangement to their smallest (S) RNA species. This S RNA codes for the viral N protein (translated from a viral-complementary mRNA) and a nonstructural protein (translated from a viral-sense mRNA). The middle-size (M) RNA of phleboviruses codes for a precursor to the viral glycoproteins (translated from a viral-complementary mRNA). The largest viral RNA (L) is presumed to code for the viral transcriptase/replicase.
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PMID:Infection and coding strategies of arenaviruses, phleboviruses, and nairoviruses. 254 46

Polypeptides have been defined by studying structural and nonstructural proteins. The rotavirus outer capsid is made up of three proteins: VP7, VP3 and VP9. VP7 is a glycoprotein involved in cell attachment and viral maturation. VP3 is associated with hemagglutination and trypsin activation of virus infectivity; both contain type-specific neutralization determinants. A biological function has not yet been completely defined for VP9. VP6, the main protein of the inner capsid is necessary for mRNA synthesis by the viral transcriptase and determines the subgroup antigenic specificity. These two capsids surround the core which consists of three proteins VP1, VP2, and the product of segment 3, associated with RNA polymerase. Four non-structural polypeptides have been identified (NCVP5, NCVP4, NCVP2, NCVP3); very little is known about their biological role.
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PMID:[Rotaviruses: structure and function of the principal polypeptides]. 255 46

The synthesis of viral proteins and S RNAs in cells infected with 12 temperature-sensitive (ts) mutants of Pichinde virus was characterized. The mutants could be divided into five groups on the basis of the patterns of radiolabeled proteins immunoprecipitated from infected-cell lysates. Markedly reduced nucleoprotein levels and undetectable amounts of glycoprotein precursor and L protein were synthesized at the nonpermissive temperature in cells infected with five of the mutants. Reduced but detectable amounts of the viral proteins were synthesized at the nonpermissive temperature in cells infected with a single mutant. Two mutants were associated with the intracellular accumulation of glycoprotein precursor, which was apparently not transported across the cell membrane in cells incubated at the nonpermissive temperature. The synthesis of viral proteins in cells infected with two mutants was indistinguishable from those produced by wild-type virus. Two additional mutants were associated with markedly reduced amounts of immunoprecipitable proteins in infected cells incubated at both the permissive and nonpermissive temperatures. Analysis of viral RNA with radiolabeled single-stranded cDNA probes representing complementary and genomic-sense sequences corresponding to the 3' region of S RNA revealed two basic patterns of viral RNA synthesis. At the nonpermissive temperature, the synthesis of complementary- and genomic-sense sequences and mRNA of the S RNA segment was markedly reduced in cells infected with representative members of these mutant groups, suggesting the presence of mutations altering transcriptase activity. Viral-complementary- and genomic-sense sequence and RNA synthesis, as well as nucleoprotein mRNA in cells, was detected in reduced amounts for mutants associated with reduced levels of proteins at both temperatures. Interestingly, RNA species larger than the S RNA segment were detected in cells infected with some of the mutants, especially those with putative transcriptase lesions. These molecules suggest a possible oligomeric intermediate in the synthesis of S RNA of Pichinde virus.
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PMID:Characterization of temperature-sensitive mutants of Pichinde virus. 317 36

A procedure has been developed for the sequential removal and purification of the glycoprotein and membrane protein of vesicular stomatitis virus (VSV). Neither of these proteins exhibited transcriptase activity. All of the activity was recovered in the ribonucleic acid (RNA)-ribonucleoprotein complex of VSV, which also has four other minor proteins associated with it. During transcription of 41% of the RNA of a virus preparation, no dissociation of the ribonucleoprotein from the viral RNA was observed.
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PMID:Dissociation of vesicular stomatitis virus and relation of the virion proteins to the viral transcriptase. 434 41


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