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

被引：2

作者：

Herr, N. ^{[1
]}

Webby, M. N. ^{[1
]}

Bulloch, E. M. M. ^{[1
]}

Schmitz, M. ^{[2
]}

Kingston, R. L. ^{[1
]}

机构：

[1] Univ Auckland, Sch Biol Sci, Auckland, New Zealand

[2] Univ Auckland, Sch Chem Sci, Auckland, New Zealand

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2019年 / 13卷 / 01期

关键词：

Rubulavirus; Negative-sense single stranded RNA viruses; RNA-dependent RNA polymerase; Intrinsically disordered proteins; TRANSCRIPTION; SPECTROSCOPY; DOMAIN; LYSINE; SYSTEM;

D O I：

10.1007/s12104-019-09876-z

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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 H-1, N-15, and C-13 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.

引用

页码：195 / 199

页数：5

共 18 条

[1] Residue-specific pKa determination of lysine and arginine side chains by indirect 15N and 13C NMR spectroscopy:: Application to apo calmodulin [J].