Mitotic phosphorylation of histone H3 at threonine 3

被引：86

作者：

Polioudaki, H

Markaki, Y

Kourmouli, N

Dialynas, G

Theodoropoulos, PA

Singh, PB

Georgatos, SD ^{[1
]}

机构：

[1] Univ Ioannina, Sch Med, Biol Lab, GR-45110 Ioannina, Greece

[2] Univ Crete, Dept Basic Sci, Sch Med, Iraklion 95110, Crete, Greece

[3] Roslin Inst, Nucl Reprogramming Lab, Dept Gene Express & Dev, Roslin EH25 9PS, Midlothian, Scotland

来源：

FEBS LETTERS | 2004年 / 560卷 / 1-3期

基金：

英国生物技术与生命科学研究理事会;

关键词：

historic; phosphorylation; heterochromatin protein 1;

D O I：

10.1016/S0014-5793(04)00060-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Nuclear envelope-peripheral heterochromatin fractions contain multiple historic 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 fie 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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：39 / 44

页数：6

共 42 条

[1] Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31 [J].