Literature DB >> 2985268

The host protein required for in vitro replication of poliovirus is a protein kinase that phosphorylates eukaryotic initiation factor-2.

C D Morrow, G F Gibbons, A Dasgupta.   

Abstract

The HeLa cell protein (host factor) required for in vitro replication of poliovirus has been identified as a 67,000 dalton phosphoprotein. The purified protein displays three activities in vitro: stimulation of poliovirus RNA synthesis in the presence of poliovirus replicase, apparent self-phosphorylation, and phosphorylation of the alpha-subunit of eukaryotic protein synthesis initiation factor 2 (eIF-2). All three activities can be removed or inhibited by an antibody to host factor. Partially purified preparations of reticulocyte eIF-2 contain a similar phosphoprotein and display host factor activity in the viral RNA synthesis assay in vitro. In vitro phosphorylation of the 67 kd protein can be stimulated by low concentrations of double-stranded RNA. Addition of phosphorylated host factor in an in vitro RNA synthesis assay significantly changes the kinetics of viral RNA synthesis, indicating that protein phosphorylation may play an important role in viral RNA replication.

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Year:  1985        PMID: 2985268     DOI: 10.1016/0092-8674(85)90351-4

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  31 in total

1.  Expression, purification, and properties of recombinant encephalomyocarditis virus RNA-dependent RNA polymerase.

Authors:  S Sankar; A G Porter
Journal:  J Virol       Date:  1991-06       Impact factor: 5.103

2.  Mechanism of in vitro synthesis of covalently linked dimeric RNA molecules by the poliovirus replicase.

Authors:  J M Lubinski; G Kaplan; V R Racaniello; A Dasgupta
Journal:  J Virol       Date:  1986-05       Impact factor: 5.103

3.  The alpha subunit of eucaryotic initiation factor 2 is phosphorylated in mengovirus-infected mouse L cells.

Authors:  J DeStefano; E Olmsted; R Panniers; J Lucas-Lenard
Journal:  J Virol       Date:  1990-09       Impact factor: 5.103

4.  Evidence for a novel signal transduction pathway activated by platelet-derived growth factor and by double-stranded RNA.

Authors:  D J Hall; S D Jones; D R Kaplan; M Whitman; B J Rollins; C D Stiles
Journal:  Mol Cell Biol       Date:  1989-04       Impact factor: 4.272

5.  The cellular 68,000-Mr protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection: implications for translational regulation.

Authors:  T L Black; B Safer; A Hovanessian; M G Katze
Journal:  J Virol       Date:  1989-05       Impact factor: 5.103

6.  Activation of double-stranded RNA-activated protein kinase in HeLa cells after poliovirus infection does not result in increased phosphorylation of eucaryotic initiation factor-2.

Authors:  L J Ransone; A Dasgupta
Journal:  J Virol       Date:  1987-06       Impact factor: 5.103

7.  A heat-sensitive inhibitor in poliovirus-infected cells which selectively blocks phosphorylation of the alpha subunit of eucaryotic initiation factor 2 by the double-stranded RNA-activated protein kinase.

Authors:  L J Ransone; A Dasgupta
Journal:  J Virol       Date:  1988-10       Impact factor: 5.103

8.  Synthesis of plus- and minus-strand RNA from poliovirion RNA template in vitro.

Authors:  T D Hey; O C Richards; E Ehrenfeld
Journal:  J Virol       Date:  1986-06       Impact factor: 5.103

9.  Multiple isoelectric forms of poliovirus RNA-dependent RNA polymerase: evidence for phosphorylation.

Authors:  L J Ransone; A Dasgupta
Journal:  J Virol       Date:  1989-11       Impact factor: 5.103

10.  Poliovirus protein 3AB forms a complex with and stimulates the activity of the viral RNA polymerase, 3Dpol.

Authors:  S J Plotch; O Palant
Journal:  J Virol       Date:  1995-11       Impact factor: 5.103

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