NMR chemical shift assignment of the C-terminal region of the Menangle virus phosphoprotein
Menangle virus is a bat-borne paramyxovirus with zoonotic potential. The single-stranded RNA genome of the virus is encapsidated in a helical nucleocapsid which is the template for both transcription and genome replication. Each of these operations is performed by the viral RNA polymerase. The phosphoprotein is the non-catalytic subunit of the polymerase, and its C-terminal region enables the polymerase to engage with the nucleocapsid. Here, we report the 1H, 15N, and 13C chemical shift assignments of the C-terminal region (amino acids 267–388) of the Menangle virus phosphoprotein. This region has a bipartite character, with a highly flexible and structurally disordered sequence preceding a structured nucleocapsid-binding domain. NMR chemical shift assignment will enable the detailed characterization of the dynamic behavior of the phosphoprotein, and its functional linkage with polymerase translocation.
KeywordsRubulavirus Negative-sense single stranded RNA viruses RNA-dependent RNA polymerase Intrinsically disordered proteins
We thank Junji Iwahara (UTMB) for the sharing of pulse programs. This work was funded by a RSNZ Marsden Grant (UOA1202).