Evidence for N-7 guanine methyl transferase activity encoded within the modular domain of RNA-dependent RNA polymerase L of a Morbillivirus

Gopinath, M and Shaila, MS (2015) Evidence for N-7 guanine methyl transferase activity encoded within the modular domain of RNA-dependent RNA polymerase L of a Morbillivirus. In: VIRUS GENES, 51 (3). pp. 356-360.

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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:	Journal Article
Publication:	VIRUS GENES
Publisher:	SPRINGER
Additional Information:	Copy right for this article belongs to the SPRINGER, VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS
Keywords:	Paramyxoviruses; Rinderpest virus; L protein; RNA-dependent RNA polymerase; N7 guanine methyl transferase; mRNA capping
Department/Centre:	Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited:	30 Dec 2015 06:03
Last Modified:	30 Dec 2015 06:03
URI:	http://eprints.iisc.ac.in/id/eprint/52938

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