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Sp1的O-连接N-乙酰葡糖胺化作用会中断Sp1与NF-Y的相互作用。

O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y.

作者信息

Lim Kihong, Chang Hyo-Ihl

机构信息

School of Life Sciences and Biotechnology, Korea University, 5-1 Anam-dong, Seongbuk-gu, Seoul 136-701, Republic of Korea.

出版信息

Biochem Biophys Res Commun. 2009 May 8;382(3):593-7. doi: 10.1016/j.bbrc.2009.03.075. Epub 2009 Mar 18.

DOI:10.1016/j.bbrc.2009.03.075
PMID:19302979
Abstract

O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation. Sp1 transcription factor is multiply modified by O-GlcNAc within its serine/threonine-rich region and glutamine-rich transactivation domain. In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription. Our results strengthen the notion that O-GlcNAc regulates gene transcription by modulating the protein-protein interaction network among transcription regulatory proteins.

摘要

O-连接的N-乙酰葡糖胺(O-GlcNAc)是一种添加在核质蛋白上的单糖N-乙酰葡糖胺,在转录调节因子中含量丰富,并与基因调控有关。Sp1转录因子在其富含丝氨酸/苏氨酸的区域和富含谷氨酰胺的反式激活结构域内被O-GlcNAc多重修饰。在本研究中,我们发现Sp1富含丝氨酸/苏氨酸区域的O-GlcNAc中断了Sp1与NF-YA之间的物理相互作用,从而抑制了Sp1-NF-Y对基因转录的协同激活。我们的结果强化了这样一种观点,即O-GlcNAc通过调节转录调节蛋白之间的蛋白质-蛋白质相互作用网络来调控基因转录。

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