来自美国芝加哥大学生物化学与分子生物学系的科学家研究解析了Mu 转位酶(MuA)与噬菌体DNA末端和靶DNA形成的复合物的结构。该结构阐释了Mu转座的复杂性。

-2012年11月15日《自然》

中文翻译


【题目】 Mu转座体结构阐明了DDE重组酶的进化

【译文】对噬菌体Mu转座的研究为理解逆转录病毒整合和V(D)J重组以及许多其他DNA转座反应奠定了基础。本研究依据各种分辨率为5.2 Å、5.2 Å和3.7 Å的参数并联合先前解析的单个结构域的结构解析了Mu转座体的结构,即Mu 转位酶(MuA)与噬菌体DNA末端和靶DNA形成的复合物的结构。该高度缠绕的结构阐明了为什么化学活性依赖于突触复合体的形成,并揭示了单个结构域当结合到不同位点时具有不同的作用。该结构也为终产物复合物增加的稳定性以及其通过ATP依赖的解叠酶ClpX产生的优先识别作用提供了解释。尽管MuA和许多其他重组酶共享了一种结构上保守的‘DDE’催化结构,但一组有限的可用复合物结构的比对表明一些保守的特征,如反向催化和靶DNA转折,通过趋同进化而形成,因为它们对功能十分重要。

英文原稿


[Title]: The Mu transpososome structure sheds light on DDE recombinase evolution

[Authors]:Sherwin P. Montaño,1 Ying Z. Pigli1 & Phoebe A. Rice1

[Abstract]Studies of bacteriophage Mu transposition paved the way for understanding retroviral integration and V(D)J recombination as well as many other DNA transposition reactions. Here we report the structure of the Mu transpososome—Mu transposase (MuA) in complex with bacteriophage DNA ends and target DNA—determined from data that extend anisotropically to 5.2 Å, 5.2 Å and 3.7 Å resolution, in conjunction with previously determined structures of individual domains. The highly intertwined structure illustrates why chemical activity depends on formation of the synaptic complex, and reveals that individual domains have different roles when bound to different sites. The structure also provides explanations for the increased stability of the final product complex and for its preferential recognition by the ATP-dependent unfoldase ClpX. Although MuA and many other recombinases share a structurally conserved ‘DDE’ catalytic domain, comparisons among the limited set of available complex structures indicate that some conserved features, such as catalysis in trans and target DNA bending, arose through convergent evolution because they are important for function.

原文地址

http://www.nature.com/nature/journal/v491/n7424/full/nature11602.html

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