http://journals.plos.org/plosone/article/figure/image?size=medium&id=info:doi/10.1371/journal.pone.0143081.g001
https://www.ncbi.nlm.nih.gov/pubmed/1656588?dopt=Abstract
bmed/1656588?dopt=Abstract
Virology. 1991 Nov;185(1):299-308.
Measles virus phosphoprotein retains the nucleocapsid protein in the cytoplasm.
Abstract
Measles virus
(MV) proteins were efficiently expressed in COS and Vero cells from
vectors based on the strong cytomegalovirus enhancer-promoter and the
simian virus 40 origin of replication. When expressed alone, nucleocapsid protein (N) migrates predominantly into the nucleus whereas phosphoprotein (P) is located in the cytoplasm. Coexpression of N and P
proteins results in retention of the N protein in the cytoplasm, as
seen also in infected cells. The retention of N protein is due to
specific interactions with the P protein since coexpression of N with either the matrix or the hemagglutinin protein had no effect. Mapping of the regions of N-P interactions on P protein revealed that the carboxy-terminal 40% of P was sufficient for specific binding to N; however, the carboxy-terminal 60% of P was required for retention of N in the cytoplasm. Thus, the V and C proteins encoded within the first half of the P
gene are not involved in the cytoplasmic retention of N protein. N
protein might be fortuitously targeted to the nucleus as a result of its
many basic amino acids, presumably destined to interact with the MV
genome. However, this set of experiments has allowed to analyze in vivo
the interactions between the N and P proteins.
- PMID:
- 1656588
- [Indexed for MEDLINE]
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