Mitotic phosphorylation of histone H3 at threonine 3

Hara Polioudaki, Yolanda Markaki, Niki Kourmouli, George Dialynas, Panayiotis A Theodoropoulos, Prim B Singh, Spyros D Georgatos

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Abstract

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.

Original languageEnglish
Pages (from-to)39-44
Number of pages6
JournalFEBS Letters
Volume560
Issue number1-3
DOIs
Publication statusPublished - Feb 27 2004

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Keywords

  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • Cell Fractionation
  • Cell Nucleus
  • Erythrocyte Membrane
  • Erythrocytes
  • Glutathione Transferase
  • Heterochromatin
  • Histones
  • Mitosis
  • Nuclear Envelope
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Recombinant Fusion Proteins
  • Threonine
  • Turkeys
  • Comparative Study
  • Journal Article
  • Research Support, Non-U.S. Gov't

Cite this

Polioudaki, H., Markaki, Y., Kourmouli, N., Dialynas, G., Theodoropoulos, P. A., Singh, P. B., & Georgatos, S. D. (2004). Mitotic phosphorylation of histone H3 at threonine 3. FEBS Letters, 560(1-3), 39-44. https://doi.org/10.1016/S0014-5793(04)00060-2