Mitotic phosphorylation of histone H3 at threonine 3

FEBS Letters

Polioudaki, Hara¹  Georgatos, Spyros D³  Kourmouli, Niki²  Markaki, Yolanda³  Dialynas, George³  Singh, Prim B²  Theodoropoulos, Panayiotis A¹ 

[1] Department of Basic Sciences, The University of Crete, School of Medicine, 95 110 Heraklion, Crete, Greece;Nuclear Reprogramming Laboratory, Department of Gene Expression and Development, The Roslin Institute, Edinburgh EH25 9PS, UK;Laboratory of Biology, The University of Ioannina, School of Medicine, 45 110 Ioannina, Greece

关键词: Histone;    Phosphorylation;    Heterochromatin protein 1;    NEPH;    nuclear envelope-peripheral heterochromatin fractions;    HP1;    heterochromatin protein 1;    NE;    nuclear envelopes;    NG;    nuclear ghosts;    SE;    salt extract;    STE;    salt/Triton extract;   

DOI  :  10.1016/S0014-5793(04)00060-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown