 |
Journal articles
Regulation of measles virus gene expression by P protein coiled-coil properties
Abstract : The polymerase of negative-stranded RNA viruses consists of the large protein (L) and the phosphoprotein (P), the latter serving both as a chaperon and a cofactor for L. We mapped within measles virus (MeV) P the regions responsible for binding and stabilizing L and showed that the coiled-coil multimerization domain (MD) of P is required for gene expression. MeV MD is kinked as a result of the presence of a stammer. Both restoration of the heptad regularity and displacement of the stammer strongly decrease or abrogate activity in a minigenome assay. By contrast, P activity is rather tolerant of substitutions within the stammer. Single substitutions at the "a" or "d" hydrophobic anchor positions with residues of variable hydrophobicity revealed that P functionality requires a narrow range of cohesiveness of its MD. Results collectively indicate that, beyond merely ensuring P oligomerization, the MD finely tunes viral gene expression through its cohesiveness.
Cited literature [102 references]
https://hal.archives-ouvertes.fr/hal-02133726
Contributor : Agnès Bussy <>
Submitted on : Monday, May 20, 2019 - 3:17:41 PM
Last modification on : Thursday, January 21, 2021 - 1:34:17 PM
Contributor : Agnès Bussy <>
Submitted on : Monday, May 20, 2019 - 3:17:41 PM
Last modification on : Thursday, January 21, 2021 - 1:34:17 PM
File
eaaw3702.full.pdf
Publication funded by an institution
Licence
Distributed under a Creative Commons Attribution - NonCommercial 4.0 International License