Sesbania mosaic virus (SeMV) polyprotein was shown to undergo proteolytic processing when expressed in E. coli. Mutational analysis of the proposed catalytic triad residues (H181, D216, and S284) present in the N-terminal serine protease domain of the polyprotein showed that the protease was indeed responsible for this processing. Analysis of the cleavage site mutants confirmed the cleavage between proteaseviral protein genome linked (VPg) and VPg-RNA-dependent RNA polymerase (RdRP) at $E^{325} - T^{326}$ and $E^{402} - T^{403}$ sites, respectively. An additional suboptimal cleavage at $E^{498} - S^{499}$ site was also identified which resulted in the further processing of RdRP to 10- and 52-kDa proteins. Thus, the protease has both E-T and...
The virus-encoded proteins of tobacco etch virus (TEV), a plant potyvirus, arise by proteolytic proc...
The C-terminal disordered domain of sesbania mosaic virus (SeMV) RNA-dependent RNA polymerase (RdRp)...
The non-structural proteins of Sindbis virus, nsP1, 2, 3 and 4, are produced upon cleavage of polypr...
AbstractSesbania mosaic virus (SeMV) polyprotein was shown to undergo proteolytic processing when ex...
Poly-protein processing is a common strategy used by many viruses to generate different functional p...
Processing of Sesbania mosaic virus (SeMV) polyprotein 2a and 2ab was reanalyzed in the view of th...
Sesbania mosaic virus (SeMV) polyprotein is processed by its N-terminal serine protease domain. The ...
Polyprotein processing is a major strategy used by many plant and animal viruses to maximize the num...
AbstractN-terminal serine protease domain of Sesbania mosaic virus polyprotein, requires fused VPg f...
N-terminal serine protease domain of Sesbania mosaic virus polyprotein, requires fused VPg for its a...
Identification of viral encoded proteins that interact with RNA-dependent RNA polymerase (RdRp) is a...
Sesbania mosaic virus (SeMV) belongs to the genus sobemovirus and it infects sesbania grandiflora pe...
Open reading frame (ORF) 2a of Sesbania mosaic virus (SeMV) codes for polyprotein 2a (Membrane anc...
AbstractOpen reading frame (ORF) 2a of Sesbania mosaic virus (SeMV) codes for polyprotein 2a (Membra...
AbstractIdentification of viral encoded proteins that interact with RNA-dependent RNA polymerase (Rd...
The virus-encoded proteins of tobacco etch virus (TEV), a plant potyvirus, arise by proteolytic proc...
The C-terminal disordered domain of sesbania mosaic virus (SeMV) RNA-dependent RNA polymerase (RdRp)...
The non-structural proteins of Sindbis virus, nsP1, 2, 3 and 4, are produced upon cleavage of polypr...
AbstractSesbania mosaic virus (SeMV) polyprotein was shown to undergo proteolytic processing when ex...
Poly-protein processing is a common strategy used by many viruses to generate different functional p...
Processing of Sesbania mosaic virus (SeMV) polyprotein 2a and 2ab was reanalyzed in the view of th...
Sesbania mosaic virus (SeMV) polyprotein is processed by its N-terminal serine protease domain. The ...
Polyprotein processing is a major strategy used by many plant and animal viruses to maximize the num...
AbstractN-terminal serine protease domain of Sesbania mosaic virus polyprotein, requires fused VPg f...
N-terminal serine protease domain of Sesbania mosaic virus polyprotein, requires fused VPg for its a...
Identification of viral encoded proteins that interact with RNA-dependent RNA polymerase (RdRp) is a...
Sesbania mosaic virus (SeMV) belongs to the genus sobemovirus and it infects sesbania grandiflora pe...
Open reading frame (ORF) 2a of Sesbania mosaic virus (SeMV) codes for polyprotein 2a (Membrane anc...
AbstractOpen reading frame (ORF) 2a of Sesbania mosaic virus (SeMV) codes for polyprotein 2a (Membra...
AbstractIdentification of viral encoded proteins that interact with RNA-dependent RNA polymerase (Rd...
The virus-encoded proteins of tobacco etch virus (TEV), a plant potyvirus, arise by proteolytic proc...
The C-terminal disordered domain of sesbania mosaic virus (SeMV) RNA-dependent RNA polymerase (RdRp)...
The non-structural proteins of Sindbis virus, nsP1, 2, 3 and 4, are produced upon cleavage of polypr...