Transcriptional Control and mRNA Capping by the GDP Polyribonucleotidyltransferase Domain of the Rabies Virus Large Protein.
Rabies virus (RABV) is a causative agent of a fatal neurological disease in humans and animals. The large (L) protein of RABV is a multifunctional RNA-dependent RNA polymerase, which is one of the most attractive targets for developing antiviral agents. A remarkable homology of the RABV L protein to a counterpart in vesicular stomatitis virus, a well-characterized rhabdovirus, suggests that it catalyzes mRNA processing reactions, such as 5'-capping, cap methylation, and 3'-polyadenylation, in addition to RNA synthesis. Recent breakthroughs in developing in vitro RNA synthesis and capping systems with a recombinant form of the RABV L protein have led to significant progress in our understanding of the molecular mechanisms of RABV RNA biogenesis. This review summarizes functions of RABV replication proteins in transcription and replication, and highlights new insights into roles of an unconventional mRNA capping enzyme, namely GDP polyribonucleotidyltransferase, domain of the RABV L protein in mRNA capping and transcription initiation.
['Ogino|Tomoaki|T|', 'Green|Todd J|TJ|']
D000818:Animals D012321:DNA-Directed RNA Polymerases D005786:Gene Expression Regulation D016679:Genome, Viral D006801:Humans D011117:Polyribonucleotide Nucleotidyltransferase D012315:RNA Caps D012367:RNA, Viral D011820:Rabies virus D012209:Rhabdoviridae D014158:Transcription, Genetic D014764:Viral Proteins D014779:Virus Replication
transcription mRNA capping GDP polyribonucleotidyltransferase rabies virus L protein de novo initiation