The C terminus of mitosin is essential for its nuclear localization, centromere/kinetochore targeting, and dimerization.
Mitosin is a novel 350-kDa nuclear phosphoprotein that dramatically relocates from the evenly nuclear distribution in S phase to the centromere/kinetochore and mitotic apparatus in M phase. The dynamic relocalization of mitosin is accompanied by the phosphorylation of itself, suggesting that mitosin plays a role in mitotic progression. The molecular ... basis of nuclear localization and targeting of mitosin to the centromere/kinetochore were characterized using a set of epitope-tagged deletion mutants. The data indicate that the extreme C terminus (amino acids 2,487-3,113) of mitosin has both an independent centromere/kinetochore targeting domain and an unusually spaced bipartite nuclear localization signal. Moreover, the same centromere/kinetochore targeting domain was shown to be essential for the ability of mitosin to bind to itself or other putative mitosin-associated proteins through use of the yeast two-hybrid system. These results suggest that the C terminus of the mitosin is essential for its role in influencing cell cycle progression.
Mesh Terms:
Amino Acid Sequence, Animals, Biological Transport, Biopolymers, Cell Line, Cell Nucleus, Centromere, Chromosomal Proteins, Non-Histone, Hela Cells, Humans, Kinetochores, Mice, Microfilament Proteins, Microscopy, Immunoelectron, Mitosis, Molecular Sequence Data, Nuclear Proteins, Phosphoproteins, Signal Transduction
Amino Acid Sequence, Animals, Biological Transport, Biopolymers, Cell Line, Cell Nucleus, Centromere, Chromosomal Proteins, Non-Histone, Hela Cells, Humans, Kinetochores, Mice, Microfilament Proteins, Microscopy, Immunoelectron, Mitosis, Molecular Sequence Data, Nuclear Proteins, Phosphoproteins, Signal Transduction
J. Biol. Chem.
Date: Aug. 18, 1995
PubMed ID: 7642639
View in: Pubmed Google Scholar
Download Curated Data For This Publication
9228
Switch View:
- Interactions 1