Mitotic phosphorylation of histone H3 at threonine 3
Mitotic phosphorylation of histone H3 at threonine 3
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DOI：
10.1016/s0014-5793(04)00060-2
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发表时间：
2004-02-27
期刊：
影响因子：
3.5
通讯作者：
Georgatos, SD
中科院分区：
文献类型：
--
作者：
Polioudaki, H;Markaki, Y;Georgatos, SD
核包膜-外周异染色质组分含有多种历史激酶活性。体外实验和氨基末端测序表明，其中一种活性与异染色质蛋白1 （HP1）共分离，并使组蛋白H3的苏氨酸3磷酸化。识别这种翻译后修饰的抗体显示，体内苏氨酸3的磷酸化开始于前期早期的5个核包膜附近，在前期扩散到周着丝粒染色质，并在后期完全逆转。这种时空模式不同于H3丝氨酸10的磷酸化，丝氨酸10也发生在细胞分裂过程中，这表明有丝分裂染色体的不同区域存在差异磷酸化的染色质分离。(C) 2004年欧洲生化学会联合会。Elsevier B.V.版权所有。
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.