Highly purified cucumber mosaic virus-induced RNA-dependent RNA polymerase does not contain any of the full length translation products of the genomic RNAs

Virology ◽  
1982 ◽  
Vol 123 (2) ◽  
pp. 284-295 ◽  
Author(s):  
Karl H.J. Gordon ◽  
Dalip S. Gill ◽  
Robert H. Symons
Keyword(s):  
Rna Polymerase ◽  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Full Length ◽  
Rna Dependent Rna Polymerase ◽  
Genomic Rnas

scholarly journals The structure of a dimeric form of SARS-CoV-2 polymerase

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Florian A. Jochheim ◽  
Dimitry Tegunov ◽  
Hauke S. Hillen ◽  
Jana Schmitzová ◽  
Goran Kokic ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Catalytic Subunit ◽  
Template Switching ◽  
Rna Dependent Rna Polymerase ◽  
Genomic Rnas ◽  
Dimeric Form

AbstractThe coronavirus SARS-CoV-2 uses an RNA-dependent RNA polymerase (RdRp) to replicate and transcribe its genome. Previous structures of the RdRp revealed a monomeric enzyme composed of the catalytic subunit nsp12, two copies of subunit nsp8, and one copy of subunit nsp7. Here we report an alternative, dimeric form of the enzyme and resolve its structure at 5.5 Å resolution. In this structure, the two RdRps contain only one copy of nsp8 each and dimerize via their nsp7 subunits to adopt an antiparallel arrangement. We speculate that the RdRp dimer facilitates template switching during production of sub-genomic RNAs.

scholarly journals Characterization of Soluble Hepatitis C Virus RNA-Dependent RNA Polymerase Expressed in Escherichia coli

1999 ◽  
Vol 73 (2) ◽  
pp. 1649-1654 ◽  
Author(s):  
Eric Ferrari ◽  
Jacquelyn Wright-Minogue ◽  
Jane W. S. Fang ◽  
Bahige M. Baroudy ◽  
Johnson Y. N. Lau ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Rna Polymerase ◽  
Nonstructural Protein ◽  
Full Length ◽  
Dependent Manner ◽  
Rdrp Activity ◽  
Rna Dependent Rna Polymerase ◽  
Hydrophobic Domain ◽  
Hcv Ns5b

ABSTRACT Production of soluble full-length nonstructural protein 5B (NS5B) of hepatitis C virus (HCV) has been shown to be problematic and requires the addition of salts, glycerol, and detergents. In an effort to improve the solubility of NS5B, the hydrophobic C terminus containing 21 amino acids was removed, yielding a truncated NS5B (NS5BΔCT) which is highly soluble and monodispersed in the absence of detergents. Fine deletional analysis of this region revealed that a four-leucine motif (LLLL) in the hydrophobic domain is responsible for the solubility profile of the full-length NS5B. Enzymatic characterization revealed that the RNA-dependent RNA polymerase (RdRp) activity of this truncated NS5B was comparable to those reported previously by others. For optimal enzyme activity, divalent manganese ions (Mn2+) are preferred rather than magnesium ions (Mg2+), whereas zinc ions (Zn2+) inhibit the RdRp activity. Gliotoxin, a known poliovirus 3D RdRp inhibitor, inhibited HCV NS5B RdRp in a dose-dependent manner. Kinetic analysis revealed that HCV NS5B has a rather low processivity compared to those of other known polymerases.

scholarly journals Full-length Dengue Virus RNA-dependent RNA Polymerase-RNA/DNA Complexes

2011 ◽  
Vol 286 (38) ◽  
pp. 33095-33108 ◽  
Author(s):  
Michal R. Szymanski ◽  
Maria J. Jezewska ◽  
Paul J. Bujalowski ◽  
Cecile Bussetta ◽  
Mengyi Ye ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Rna Polymerase ◽  
Full Length ◽  
Rna Dependent Rna Polymerase ◽  
Dna Complexes ◽  
Virus Rna
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