Chain Initiation by Reovirus RNA Transcriptase in vitro

Dh, Levin; Acs, George; Sc, Silverstein

doi:10.1038/227603a0

Cited by 24 publications

(4 citation statements)

References 23 publications

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“…We cannot explain these differences. However, a similar variation in the 5' guanosine nucleotides recovered from in vitro synthesized ssRNA has been reported (4,17,19) and has been attributed to the presence of nucleotide phosphohydrolases within the virion (4,10,16,19).…”

Section: Discussionsupporting

confidence: 59%

Synthesis of Reovirus Oligo Adenylic Acid In Vivo and In Vitro

Silverstein

Astell

Christman

et al. 1974

J Virol

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Section: Discussionsupporting

confidence: 59%

Synthesis of Reovirus Oligo Adenylic Acid In Vivo and In Vitro

Silverstein

Astell

Christman

et al. 1974

J Virol

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“…. as 5' termini resembles the situation with reovirus, since the multiple double strands of the RNA of this virus were found to carry both pppG and ppG termini (Levin et al, 1970). The possible role of the nucleoside triphosphate hydrolases of that virus in producing the pp-G termini was discussed by Kapuler et al (1970), and similar enzymes might be sought in STNV-infected plants.…”

Section: Discussionmentioning

confidence: 95%

Terminal heterogeneity at both ends of the satellite tobacco necrosis virus ribonucleic acid

Horst¹,

Fraenkel‐Conrat²,

Mandeles³

1971

Biochemistry

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The end groups of the RNA of the satellite of tobacco necrosis virus (STNV) were analyzed by Sanger's methods. The 5'-terminal AGUwas found to be present in both the 5'-diphosphorylated and -triphosphorylated states. The 3'-terminal sequence was found to be -GACUACCC. Since all viral RNA preparations that have been analyzed terminate T X he small size of satellite tobacco necrosis virus (STNV)-RNA,1 in comparison with other viral RNAs, as well as its dependence on a helper virus (TNV), has made this virus attractive for sequence analysis studies. From sedimentation investigations, an RNA chain length of 1200 nucleotides can be calculated. If all of these nucleotides were used to code for amino acids in a protein, STNV-RNA could serve as a message for 400 amino acids. The molecular weight of STNV coat protein has been estimated at approximately 20,000-22,000 (Lesnaw and Reichmann, 1970;Rees et al., 1970). This implies a protein chain length of about 190 amino acids and leaves room for a second cistron of equal size if all of the STNV-RNA serves as a translatable messenger.Previous sequence studies of STNV-RNA have provided evidence for the sequences ppApGpUp at the 5' end (Wimmer et al., 1968), and -G(U,2AC)C as well as -G(U,2AC,C)C at the 3' end (Wimmer and Reichmann, 1969).2 As part of a contemplated program of complete sequence elucidation of this RNA by means of the two-dimensional analysis system (Sanger et al., 1965), the terminal oligonucleotides have now been reinvestigated. The 5' sequence was confirmed, although it was found to be in part triphosphorylated. The 3'-terminal octanucleotide sequence was established. A preliminary report of the results of

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“…Previous studies indicated that the MRV cores serve as transcriptase particle in vivo and transcriptionally active in vitro for the production of plus-strand RNAs [ 56 , 57 , 58 , 59 ]. In this study, based on the fact that aquareovirus inner-capsid proteins were retained within VIBs during infection, it would be suggested that newly synthesized viral RNAs are located within VIBs.…”

Section: Discussionmentioning

confidence: 99%

Aquareovirus NS80 Initiates Efficient Viral Replication by Retaining Core Proteins within Replication-Associated Viral Inclusion Bodies

et al. 2015

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Viral inclusion bodies (VIBs) are specific intracellular compartments for reoviruses replication and assembly. Aquareovirus nonstructural protein NS80 has been identified to be the major constituent for forming globular VIBs in our previous study. In this study, we investigated the role of NS80 in viral structural proteins expression and viral replication. Immunofluorescence assays showed that NS80 could retain five core proteins or inner-capsid proteins (VP1-VP4 and VP6), but not outer-capsid proteins (VP5 and VP7), within VIBs in co-transfected or infected cells. Further co-immunoprecipitation analysis confirmed that NS80 could interact with each core protein respectively. In addition, we found that newly synthesized viral RNAs co-localized with VIBs. Furthermore, time-course analysis of viral structural proteins expression showed that the expression of NS80 was detected first, followed by the detection of inner shell protein VP3, and then of other inner-capsid proteins, suggesting that VIBs were essential for the formation of viral core frame or progeny virion. Moreover, knockdown of NS80 by shRNA not only inhibited the expression of aquareovirus structural proteins, but also inhibited viral infection. These results indicated that NS80-based VIBs were formed at earlier stage of infection, and NS80 was able to coordinate the expression of viral structural proteins and viral replication.

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Chain Initiation by Reovirus RNA Transcriptase in vitro

Cited by 24 publications

References 23 publications

Synthesis of Reovirus Oligo Adenylic Acid In Vivo and In Vitro

Synthesis of Reovirus Oligo Adenylic Acid In Vivo and In Vitro

Terminal heterogeneity at both ends of the satellite tobacco necrosis virus ribonucleic acid

Aquareovirus NS80 Initiates Efficient Viral Replication by Retaining Core Proteins within Replication-Associated Viral Inclusion Bodies

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