A novel fold in the TraI relaxase-helicase c-terminal domain is essential for conjugative DNA transfer.

A novel fold in the TraI relaxase-helicase c-terminal domain is essential for conjugative DNA transfer.
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DOI:
10.1016/j.jmb.2008.12.057
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发表时间:
2009-02-20
影响因子:
5.6
通讯作者:
Redinbo, Matthew R.
Redinbo, Matthew R.
中科院分区:
生物学2区
文献类型:
--
作者:
Guogas, Laura M.;Kennedy, Sarah A.;Lee, Jin-Hyup;Redinbo, Matthew R.

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TRAI松弛酶-解旋酶是多蛋白松弛小体复合体的中心催化成分,负责细菌细胞之间的接合DNA转移(CDT)。CDT是微生物遗传物质横向繁殖的主要机制,包括抗生素耐药基因的传播。给出了多功能大肠杆菌F质粒Trai蛋白(Trai-CT)C-末端结构域的2.4?分辨率晶体结构,并鉴定了CDT所必需的特定结构区域。晶体结构揭示了由28个残基的N末端α结构域通过富含脯氨酸的环连接到紧凑的α/β结构域组成的新折叠。α/β结构域的球状性质和富含脯氨酸的环的存在和刚性都是进行DNA转移和单链DNA结合所必需的。综上所述,这些数据确定了这个非催化结构域的特定结构特征,这些结构特征对于DNA结合是必不可少的。
The TraI relaxase-helicase is the central catalytic component of the multi-protein relaxosome complex responsible for conjugative DNA transfer (CDT) between bacterial cells. CDT is a primary mechanism for the lateral propagation of microbial genetic material, including the spread of antibiotic resistance genes. The 2.4 Å resolution crystal structure of the C-terminal domain of the multifunctional Escherichia coli F plasmid TraI protein (TraI-CT) is presented, and specific structural regions essential for CDT are identified. The crystal structure reveals a novel fold composed of a 28-residue N-terminal α-Domain connected by a proline-rich loop to a compact α/β-Domain. Both the globular nature of the α/β-Domain and the presence and rigidity of the proline-rich loop are required for DNA transfer and single-stranded DNA binding. Taken together, these data establish the specific structural features of this non-catalytic domain that are essential to DNA conjugation.
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发表时间: 2004-12-01
影响因子: 2.2
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