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重组介导蛋白RecR中Cys4锌指基序的结构与功能表征

Structural and functional characterization of Cys4 zinc finger motif in the recombination mediator protein RecR.

作者信息

Tang Qun, Liu Yan-Ping, Yan Xiao-Xue, Liang Dong-Cai

机构信息

National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

出版信息

DNA Repair (Amst). 2014 Dec;24:10-14. doi: 10.1016/j.dnarep.2014.09.012.

Abstract

Zinc finger motif widely exists in protein structure, which can play different roles in different proteins. RecR is an important recombination mediator protein (RMP) in the RecFOR pathway and zinc finger motif is the most conserved domain in RecR protein. However, the function of this zinc finger motif in RecR is unclear. Here, we have studied the structures of the single cysteine and double cysteines mutation within the zinc finger motif in Thermoanaerobacter tengcongensis RecR (TTERecR). We have also studied the DNA binding ability as well as TTERecO protein binding ability of single, double and even triple cysteines mutation of the zinc finger motif, and the mutants do not alter DNA binding by RecR nor the interaction between RecR and RecO. The function of TTERecR zinc finger motif is to maintain the stability of the three-dimensional structure.

摘要

锌指基序广泛存在于蛋白质结构中,它在不同蛋白质中发挥着不同作用。RecR是RecFOR途径中的一种重要重组介导蛋白(RMP),锌指基序是RecR蛋白中最保守的结构域。然而,该锌指基序在RecR中的功能尚不清楚。在此,我们研究了嗜热栖热放线菌RecR(TTERecR)锌指基序内单半胱氨酸和双半胱氨酸突变体的结构。我们还研究了锌指基序单、双甚至三半胱氨酸突变体的DNA结合能力以及与TTERecO蛋白的结合能力,这些突变体不会改变RecR与DNA的结合,也不会改变RecR与RecO之间的相互作用。TTERecR锌指基序的功能是维持三维结构的稳定性。

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