Figure 2. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of recombinant wild-type (WT) and mutant VSV L proteins. The WT.

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Figure 2. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of recombinant wild-type (WT) and mutant VSV L proteins. The WT and mutant VSV L proteins (1 μg) were analyzed by 7.5% SDS-PAGE followed by Coomassie Brilliant Blue staining. M lanes show marker proteins with the indicated molecular masses. The names of the point mutants contain the original amino acid (one-letter code) at the indicated position in the VSV L protein followed by the replacement amino acid. The HR-RH mutant carrying the H1227R and R1228H mutations (lane 33) is a representative of the previously identified cap-defective mutants (16). From: Signature motifs of GDP polyribonucleotidyltransferase, a non-segmented negative strand RNA viral mRNA capping enzyme, domain in the L protein are required for covalent enzyme–pRNA intermediate formation Nucleic Acids Res. 2015;44(1):330-341. doi:10.1093/nar/gkv1286 Nucleic Acids Res | © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. 1