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Ets-1/Pax5复合物在DNA上形成的结构研究。

Structural studies of Ets-1/Pax5 complex formation on DNA.

作者信息

Garvie C W, Hagman J, Wolberger C

机构信息

Department of Biophysics and Biophysical Chemistry, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.

出版信息

Mol Cell. 2001 Dec;8(6):1267-76. doi: 10.1016/s1097-2765(01)00410-5.

DOI:10.1016/s1097-2765(01)00410-5
PMID:11779502
Abstract

Pax5 regulates the B cell-specific expression of the mb-1 gene together with members of the Ets family of transcriptional activators. The Ets proteins on their own bind poorly to the Pax5/Ets binding site, but can be recruited to the site by cooperative interactions with Pax5. The structure of the ETS domain of Ets-1 and the paired domain of Pax5 bound to DNA reveals the molecular details of the selective recruitment of different Ets proteins by Pax5. Comparison with structures of Ets-1 alone bound to both high- and low-affinity DNA sites reveals that Pax5 alters the Ets-1 contacts with DNA. The ability of one protein to alter the DNA sequence-specific contacts of another provides a general mechanism for combinatorial regulation of transcription.

摘要

Pax5与转录激活因子Ets家族成员共同调节mb-1基因的B细胞特异性表达。Ets蛋白自身与Pax5/Ets结合位点的结合能力较差,但可通过与Pax5的协同相互作用被招募至该位点。Ets-1的ETS结构域与结合DNA的Pax5的配对结构域的结构揭示了Pax5对不同Ets蛋白进行选择性招募的分子细节。将Ets-1单独结合高亲和力和低亲和力DNA位点的结构进行比较,发现Pax5改变了Ets-1与DNA的接触。一种蛋白质改变另一种蛋白质与DNA序列特异性接触的能力为转录的组合调控提供了一种普遍机制。

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