噬菌体P4衣壳蛋白(Psu)作为转录抗终结者的兼职功能。

Bacteriophage Pub Date : 2013-04-01 DOI:10.4161/bact.25657
Amitabh Ranjan, Ramanuj Banerjee, Bibhusita Pani, Udayditya Sen, Ranjan Sen
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引用次数: 9

摘要

Psu是一种20-kD噬菌体P4衣壳修饰蛋白,作为rho依赖性终止的转录抗终止剂。Psu与大肠杆菌Rho蛋白形成特异性复合物,并影响后者沿新生RNA的atp依赖性转位酶活性。形成独特的打结二聚体,呈v型结构。Psu的c端螺旋与Rho的无序区有特定的接触,包括残基139-153。Rho-Psu配合物的能量最小化结构模型表明,v形Psu二聚体在Rho六聚体的中央通道上形成一个盖子。Psu的这种构型对Rho的转位酶活性造成了机械障碍。了解Psu抑制Rho作用的结构和机制基础可能有助于设计针对细菌Rho依赖的转录终止过程的肽抑制剂。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

The moonlighting function of bacteriophage P4 capsid protein, Psu, as a transcription antiterminator.

The moonlighting function of bacteriophage P4 capsid protein, Psu, as a transcription antiterminator.

The moonlighting function of bacteriophage P4 capsid protein, Psu, as a transcription antiterminator.

The moonlighting function of bacteriophage P4 capsid protein, Psu, as a transcription antiterminator.

Psu, a 20-kD bacteriophage P4 capsid decorating protein moonlights as a transcription antiterminator of the Rho-dependent termination. Psu forms specific complex with E.coli Rho protein, and affects the latter's ATP-dependent translocase activity along the nascent RNA. It forms a unique knotted dimer to take a V-shaped structure. The C-terminal helix of Psu makes specific contacts with a disordered region of Rho, encompassing the residues 139-153. An energy minimized structural model of the Rho-Psu complex reveals that the V-shaped Psu dimer forms a lid over the central channel of the Rho hexamer. This configuration of Psu causes a mechanical impediment to the translocase activity of Rho. The knowledge of structural and mechanistic basis of inhibition of Rho action by Psu may help to design peptide inhibitors for the conserved Rho-dependent transcription termination process of bacteria.

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