Localization of MPM-2 recognized phosphoproteins and tubulin during cell cycle progression in synchronized Vicia faba root meristem cells
Language English Country Great Britain, England Media print
Document type Journal Article
PubMed
8220311
DOI
10.1006/cbir.1993.1147
PII: S1065-6995(83)71147-9
Knihovny.cz E-resources
- MeSH
- Spindle Apparatus chemistry ultrastructure MeSH
- Cell Nucleus chemistry ultrastructure MeSH
- Cell Cycle MeSH
- Fabaceae chemistry cytology immunology MeSH
- Phosphoproteins analysis immunology MeSH
- Stem Cells chemistry ultrastructure MeSH
- Cells, Cultured MeSH
- Plants, Medicinal * MeSH
- Antibodies, Monoclonal immunology MeSH
- Plant Proteins analysis immunology MeSH
- Tubulin analysis immunology MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Phosphoproteins MeSH
- Antibodies, Monoclonal MeSH
- Plant Proteins MeSH
- Tubulin MeSH
MPM-2 antibody reacts with a subset of mitotic phosphoproteins. We followed localization of MPM-2 immunoreactive material and localization of microtubules during cell cycle progression in a highly synchronous population of Vicia faba root meristem cells and isolated nuclei. The MPM-2 antibody labelling showed significant cell cycle dependence. MPM-2 nuclear reactivity was weak and homogeneous in G1 and S phase of the cell cycle and became stronger and heterogeneous during G2, resembling staining of the nuclear matrix, with maximum staining at the G2/M interface. Similarly the staining intensity of nucleoli increased from late G1 phase to nucleoli dispersion in early prophase. During mitosis MPM-2 immunoreactivity was associated with spindle configurations and the brightest signal was localized in kinetochores from prophase to metaphase.
References provided by Crossref.org
Plant gamma-tubulin interacts with alphabeta-tubulin dimers and forms membrane-associated complexes
Nuclear gamma-tubulin during acentriolar plant mitosis