Join us for the 1st Symposium on Interconnections and Cross-Regulation of Gene Expression Processes this September in Göttingen! Great Lineup of international speakers and plenty of opportunities for early career researchers to present & discuss their work!
Link: sfb1565.uni-goettingen.de/symposion/

Looks familiar - also from a FLAG IP in HEK cells.

Comparisons between the two structures show how rearrangements of key elements in the RdRp upon RNA binding lead to large-scale reorganisation of the complex and ordering of the C-terminal domains required for RNA capping.

The structure reveals how NiV RdRp interacts with template and product RNA and with the incoming substrate nucleoside triphosphate during RNA synthesis. To our knowledge, this represents the first structure of a non-segmented negative-strand RNA virus RdRp in this state.

By using a non-hydrolyzable GTP-analog, we were additionally able to visualise the RdRp after de novo synthesis of 9 nt of product RNA. In this early replicating state, the C-terminal domains of L become stabilised and visible in the cryo-EM reconstruction.

The NiV RNA-dependent RNAP (RdRp) adopts an architecture similar to that of other negative strand RNA viruses such as Ebola or RSV, in which four copies of P protein protrude from the core formed by L. In the apo state, the C-terminal domains of L are mobile and hence invisible.