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ELECTRON MICROSCOPIC VISUALIZATION OF RECT PROTEIN AND ITS COMPLEXES WITH DNA

机译:蛋白质及其与DNA复合物的电子显微镜观察

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Electron microscopy has been used to examine Escherichia coli RecT protein alone and in the complexes it forms with DNA substrates, with which it catalyzes strand exchange in vitro. Negative staining has revealed that the 33 kDa RecT protein monomers form open C-shaped and closed O-shaped particles. RecT protein monomers assemble into donut-shaped oligomers containing seven or eight protein monomers and rod-like structures. When bound to single-stranded DNA, RecT forms highly twisted nucleoprotein filaments that are 18 nm in diameter and have a helical pitch of 10 nm. When added to linear duplex DNA in the presence of active RecE protein (exonuclease VIII), filamentous nucleoprotein complexes are formed on the DNA ends and the DNA molecules are frequently cyclized through protein-protein interactions. (C) 1995 Academic Press Limited [References: 33]
机译:电子显微镜已被用于单独检查大肠杆菌RecT蛋白,以及与DNA底物形成的复合物,可在体外催化链交换。负染色显示33 kDa RecT蛋白单体形成开放的C形和封闭的O形颗粒。 RecT蛋白单体组装成包含七个或八个蛋白单体和棒状结构的甜甜圈形低聚物。当与单链DNA结合时,RecT会形成高度扭曲的核蛋白丝,直径为18 nm,螺旋间距为10 nm。当在活性RecE蛋白(核酸外切酶VIII)存在下添加至线性双链DNA时,在DNA末端形成丝状核蛋白复合物,并且DNA分子经常通过蛋白质-蛋白质相互作用而环化。 (C)1995 Academic Press Limited [参考文献:33]

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