The N-terminal domain of the replication initiator protein RepE is a dimerization domain forming a stable dimer.
The N-terminal domain of the replication initiator protein RepE is a dimerization domain forming a stable dimer.
复制标题
复制起始蛋白RepE的N端结构域是形成稳定二聚体的二聚化结构域。
DOI：
10.1016/j.bbrc.2004.01.018
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发表时间：
2004
影响因子：
3.1
通讯作者：
K. Miki
中科院分区：
文献类型：
--
作者：
A. Nakamura;H. Komori;G. Kobayashi;A. Kita;C. Wada;K. Miki
大肠杆菌中mini-F质粒的起始蛋白RepE在DNA复制中起着重要作用，其受分子伴侣依赖的寡聚状态（单体或二聚体）的调节。交联，超离心，和凝胶过滤分析表明，唯一表达的N-末端结构域（残基1-144或1-152）存在于二聚体状态，在野生型RepE蛋白。这一结果表明，N-末端结构域作为一个二聚化结构域的RepE和可能是重要的相互作用与分子伴侣。N-末端结构域二聚体已结晶，以获得结构上的洞察RepE的单体/二聚体转化的调节。
The initiator protein RepE of the mini-F plasmid in Escherichia coli plays an essential role in DNA replication, which is regulated by the molecular chaperone-dependent oligomeric state (monomer or dimer). Crosslinking, ultracentrifugation, and gel filtration analyses showed that the solely expressed N-terminal domain (residues 1–144 or 1–152) exists in the dimeric state as in the wild-type RepE protein. This result indicates that the N-terminal domain functions as a dimerization domain of RepE and might be important for the interaction with the molecular chaperones. The N-terminal domain dimer has been crystallized in order to obtain structural insight into the regulation of the monomer/dimer conversion of RepE.