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. 2019 Apr;13(1):195-199.
doi: 10.1007/s12104-019-09876-z. Epub 2019 Jan 24.

NMR chemical shift assignment of the C-terminal region of the Menangle virus phosphoprotein

N Herr  1 , M N Webby  1 , E M M Bulloch  1 , M Schmitz  2 , R L Kingston  3
Affiliations

NMR chemical shift assignment of the C-terminal region of the Menangle virus phosphoprotein

N Herr et al. Biomol NMR Assign. 2019 Apr.

Abstract

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.

Keywords: Intrinsically disordered proteins; Negative-sense single stranded RNA viruses; RNA-dependent RNA polymerase; Rubulavirus.

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