Production of polyomavirus structural protein VP1 in yeast cells and its interaction with cell structures
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
10930583
DOI
10.1016/s0014-5793(00)01787-7
PII: S0014-5793(00)01787-7
Knihovny.cz E-resources
- MeSH
- Spindle Apparatus chemistry metabolism MeSH
- Cell Division MeSH
- Cell Nucleus chemistry metabolism MeSH
- Cell Line MeSH
- DNA, Fungal genetics metabolism MeSH
- Microscopy, Electron MeSH
- Fluorescent Antibody Technique, Indirect MeSH
- Capsid biosynthesis genetics metabolism ultrastructure MeSH
- Mice MeSH
- Recombinant Proteins biosynthesis genetics metabolism ultrastructure MeSH
- Saccharomyces cerevisiae cytology genetics metabolism ultrastructure MeSH
- Blotting, Southern MeSH
- Spodoptera MeSH
- Tubulin metabolism MeSH
- Protein Binding MeSH
- Capsid Proteins * MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- DNA, Fungal MeSH
- Recombinant Proteins MeSH
- Tubulin MeSH
- Capsid Proteins * MeSH
- VP1 protein, polyomavirus MeSH Browser
The gene for mouse polyomavirus major structural protein VP1 was expressed in Saccharomyces cerevisiae from the inducible GAL7 promoter. VP1 pseudocapsids were purified from cell lysates. Their subpopulation contained fragments of host DNA, which, in contrast to those of VP1 pseudocapsids produced in insect cells, did not assemble with cellular histones into pseudonucleocores. VP1 pseudocapsids accumulated in the yeast cell nuclei. A strong interaction of VP1 with tubulin fibres of the mitotic spindle was observed. The fibres of spindles were larger in diameter, apparently due to tight VP1 binding. Substantial growth inhibition of yeast cells producing VP1 was observed.
References provided by Crossref.org
Microtubules in Polyomavirus Infection
