Mitotic phosphorylation of histone H3 at threonine 3
| Autor: | Polioudaki, H., Markaki, Y., Kourmouli, N., Dialynas, G., Theodoropoulos, P. A., Singh, P. B., Georgatos, S. D. |
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| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Blotting
Western Mitosis Cell Fractionation Erythrocytes/cytology Nuclear Envelope/chemistry Animals Heterochromatin/chemistry Glutathione Transferase/metabolism Amino Acid Sequence Turkeys/blood Cell Nucleus/chemistry Histones/chemistry/*metabolism Phosphorylation Protein Processing Post-Translational/immunology Recombinant Fusion Proteins/chemistry/metabolism Erythrocyte Membrane/chemistry Threonine/*metabolism |
| Popis: | Nuclear envelope-peripheral heterochromatin fractions contain multiple histone kinase activities. In vitro assays and amino-terminal sequencing show that one of these activities co-isolates with heterochromatin protein 1 (HP1) and phosphorylates histone H3 at threonine 3. Antibodies recognizing this post-translational modification reveal that in vivo phosphorylation at threonine 3 commences at early prophase in the vicinity of the nuclear envelope, spreads to pericentromeric chromatin during prometaphase and is fully reversed by late anaphase. This spatio-temporal pattern is distinct from H3 phosphorylation at serine 10, which also occurs during cell division, suggesting segregation of differentially phosphorylated chromatin to different regions of mitotic chromosomes. FEBS Lett |
| Databáze: | OpenAIRE |
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