Ensemble structure of the modular and flexible full-length vesicular stomatitis virus phosphoprotein.
The phosphoprotein (P) is an essential component of the viral replication machinery of non-segmented negative-strand RNA viruses, connecting the viral polymerase to its nucleoprotein-RNA template and acting as a chaperone of the nucleoprotein by preventing nonspecific encapsidation of cellular RNAs. The phosphoprotein of vesicular stomatitis virus (VSV) forms homodimers and possesses a modular organization comprising two stable, well-structured domains concatenated with two intrinsically disordered regions. Here, we used a combination of nuclear magnetic resonance spectroscopy and small-angle X-ray scattering to depict VSV P as an ensemble of continuously exchanging conformers that captures the dynamic character of this protein. We discuss the implications of the dynamics and the large conformational space sampled by VSV P in the assembly and functioning of the viral transcription/replication machinery.
Unit of Virus Host Cell Interactions, UMI 3265 UJF-EMBL-CNRS, 6 rue Jules Horowitz, BP 181, 38042 Grenoble Cedex 9, France.
Cédric
C
Leyrat
Robert
R
Schneider
Euripedes A
EA
Ribeiro
Filip
F
Yabukarski
Mingxi
M
Yao
Francine C A
FC
Gérard
Malene Ringkjøbing
MR
Jensen
Rob W H
RW
Ruigrok
Martin
M
Blackledge
Marc
M
Jamin
D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D012367:RNA, Viral / Q000737:chemistry / Q000378:metabolism; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000737:chemistry* / Q000378:metabolism; D014779:Virus Replication
D010750:Phosphoproteins; D012367:RNA, Viral; D015678:Viral Structural Proteins