Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 423, Issue 2, Pages 182-197Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2012.07.003
Keywords
phosphoprotein; intrinsically disordered regions; vesicular stomatitis virus; NMR; SAXS
Categories
Funding
- French National Research Agency (ANR) [ANR-07-001-01]
- FINOVI foundation
- Lyonbiopole
- Human Frontier Science Program [LT000322/2011-L]
- ANR
- FINOVI
- French government
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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. (C) 2012 Elsevier Ltd. All rights reserved.
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