Putative domain-domain interactions in the vesicular stomatitis virus L polymerase protein appendage region.

ABSTRACT:

Unlabelled

The multidomain polymerase protein (L) of nonsegmented negative-strand (NNS) RNA viruses catalyzes transcription and replication of the virus genome. The N-terminal half of the protein forms a ring-like polymerase structure, while the C-terminal half encoding viral mRNA transcript modifications consists of a flexible appendage with three distinct globular domains. To gain insight into putative transient interactions between L domains during viral RNA synthesis, we exchanged each of the four distinct regions encompassing the appendage region of vesicular stomatitis virus (VSV) Indiana serotype L protein with their counterparts from VSV New Jersey and analyzed effects on virus polymerase activity in a minigenome system. The methyltransferase domain exchange yielded a fully

SUBMITTER: Ruedas JB 

PROVIDER: S-EPMC4249160 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature