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丝裂原活化蛋白激酶介导的组蛋白H3磷酸乙酰化与诱导基因调控。

MAP kinase-mediated phosphoacetylation of histone H3 and inducible gene regulation.

作者信息

Clayton Alison L, Mahadevan Louis C

机构信息

Nuclear Signalling Laboratory, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.

出版信息

FEBS Lett. 2003 Jul 3;546(1):51-8. doi: 10.1016/s0014-5793(03)00451-4.

Abstract

That signalling pathways, particularly the mitogen-activated protein kinase cascades, elicit modification of chromatin proteins such as histone H3 by phosphorylation and/or acetylation concomitant with gene activation is now well established. The picture that is emerging is one of a complex and dynamic pattern of multiple modifications at the H3 tail. Here, we review the inducible gene systems where H3 modifications have been reported and re-evaluate the controversy as to the kinase(s) that phosphorylates it as well as the proposed coupling between H3 phosphorylation and acetylation.

摘要

信号通路,尤其是丝裂原活化蛋白激酶级联反应,通过磷酸化和/或乙酰化作用引发染色质蛋白(如组蛋白H3)的修饰,同时伴随基因激活,这一点现已得到充分证实。目前呈现出的情况是H3尾部存在复杂且动态的多种修饰模式。在此,我们回顾了已报道有H3修饰的可诱导基因系统,并重新评估了关于磷酸化H3的激酶以及所提出的H3磷酸化与乙酰化之间偶联关系的争议。

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