Evidence for N7 guanine methyl transferase activity encoded within the modular domain of RNA-dependent RNA polymerase L of a Morbillivirus

Gopinath, M. ; Shaila, M. S. (2015) Evidence for N7 guanine methyl transferase activity encoded within the modular domain of RNA-dependent RNA polymerase L of a Morbillivirus Virus Genes, 51 (3). pp. 356-360. ISSN 0920-8569

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Official URL: https://link.springer.com/article/10.1007/s11262-0...

Related URL: http://dx.doi.org/10.1007/s11262-015-1252-3

Abstract

Post-transcriptional modification of viral mRNA is essential for the translation of viral proteins by cellular translation machinery. Due to the cytoplasmic replication of Paramyxoviruses, the viral-encoded RNA-dependent RNA polymerase (RdRP) is thought to possess all activities required for mRNA capping and methylation. In the present work, using partially purified recombinant RNA polymerase complex of rinderpest virus expressed in insect cells, we demonstrate the in vitro methylation of capped mRNA. Further, we show that a recombinant C-terminal fragment (1717–2183 aa) of L protein is capable of methylating capped mRNA, suggesting that the various post-transcriptional activities of the L protein are located in independently folding domains.

Item Type:Article
Source:Copyright of this article belongs to Springer-Verlag.
Keywords:Paramyxoviruses; Rinderpest Virus; L Protein; RNA-dependent RNA Polymerase; N7 Guanine Methyl Transferase; mRNA Capping
ID Code:112251
Deposited On:31 Jan 2018 04:06
Last Modified:31 Jan 2018 04:06

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