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

Research output: Contribution to journalArticle

76 Citations (Scopus)

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

Fingerprint

Phosphorylation
Nuclear Envelope
Threonine
Histones
Chromatin
Protamine Kinase
Prometaphase
Prophase
Anaphase
Heterochromatin
Post Translational Protein Processing
Chromosomes
Cell Division
Serine
Assays
Cells
Antibodies
In Vitro Techniques
heterochromatin-specific nonhistone chromosomal protein HP-1

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

Mitotic phosphorylation of histone H3 at threonine 3. / Polioudaki, Hara; Markaki, Yolanda; Kourmouli, Niki; Dialynas, George; Theodoropoulos, Panayiotis A; Singh, Prim B; Georgatos, Spyros D.

In: FEBS Letters, Vol. 560, No. 1-3, 27.02.2004, p. 39-44.

Research output: Contribution to journalArticle

Polioudaki, H, Markaki, Y, Kourmouli, N, Dialynas, G, Theodoropoulos, PA, Singh, PB & Georgatos, SD 2004, 'Mitotic phosphorylation of histone H3 at threonine 3', FEBS Letters, vol. 560, no. 1-3, pp. 39-44. https://doi.org/10.1016/S0014-5793(04)00060-2
Polioudaki H, Markaki Y, Kourmouli N, Dialynas G, Theodoropoulos PA, Singh PB et al. Mitotic phosphorylation of histone H3 at threonine 3. FEBS Letters. 2004 Feb 27;560(1-3):39-44. https://doi.org/10.1016/S0014-5793(04)00060-2
Polioudaki, Hara ; Markaki, Yolanda ; Kourmouli, Niki ; Dialynas, George ; Theodoropoulos, Panayiotis A ; Singh, Prim B ; Georgatos, Spyros D. / Mitotic phosphorylation of histone H3 at threonine 3. In: FEBS Letters. 2004 ; Vol. 560, No. 1-3. pp. 39-44.
@article{2118a428511040f4b4f3b48be09d6ed7,
title = "Mitotic phosphorylation of histone H3 at threonine 3",
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.",
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",
author = "Hara Polioudaki and Yolanda Markaki and Niki Kourmouli and George Dialynas and Theodoropoulos, {Panayiotis A} and Singh, {Prim B} and Georgatos, {Spyros D}",
year = "2004",
month = "2",
day = "27",
doi = "10.1016/S0014-5793(04)00060-2",
language = "English",
volume = "560",
pages = "39--44",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1-3",

}

TY - JOUR

T1 - Mitotic phosphorylation of histone H3 at threonine 3

AU - Polioudaki, Hara

AU - Markaki, Yolanda

AU - Kourmouli, Niki

AU - Dialynas, George

AU - Theodoropoulos, Panayiotis A

AU - Singh, Prim B

AU - Georgatos, Spyros D

PY - 2004/2/27

Y1 - 2004/2/27

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Animals

KW - Blotting, Western

KW - Cell Fractionation

KW - Cell Nucleus

KW - Erythrocyte Membrane

KW - Erythrocytes

KW - Glutathione Transferase

KW - Heterochromatin

KW - Histones

KW - Mitosis

KW - Nuclear Envelope

KW - Phosphorylation

KW - Protein Processing, Post-Translational

KW - Recombinant Fusion Proteins

KW - Threonine

KW - Turkeys

KW - Comparative Study

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1016/S0014-5793(04)00060-2

DO - 10.1016/S0014-5793(04)00060-2

M3 - Article

C2 - 14987995

VL - 560

SP - 39

EP - 44

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1-3

ER -