关于“人类DNA引发酶的[4Fe4S]簇作为利用DNA电荷传输的氧化还原开关”的评论
Comment on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".
作者信息
Baranovskiy Andrey G, Babayeva Nigar D, Zhang Yinbo, Blanco Luis, Pavlov Youri I, Tahirov Tahir H
机构信息
Eppley Institute for Research in Cancer and Allied Diseases, Fred and Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198, USA.
Department of Immunology, University of Washington, Seattle WA 98195, USA.
出版信息
Science. 2017 Jul 21;357(6348). doi: 10.1126/science.aan2396.
Abstract
O'Brien (Research Article, 24 February 2017, eaag1789) proposed a novel mechanism of primase function based on redox activity of the iron-sulfur cluster buried inside the C-terminal domain of the large primase subunit (p58C). Serious problems in the experimental design and data interpretation raise concerns about the validity of the conclusions.
摘要
奥布赖恩（研究文章，2017年2月24日，eaag1789）基于埋藏在大型引发酶亚基（p58C）C末端结构域内的铁硫簇的氧化还原活性，提出了一种引发酶功能的新机制。实验设计和数据解读中的严重问题引发了对这些结论有效性的担忧。
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Comment on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".关于“人类DNA引发酶的[4Fe4S]簇作为利用DNA电荷传输的氧化还原开关”的评论
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本文引用的文献
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The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport.人类DNA引发酶的[4Fe4S]簇通过DNA电荷传输发挥氧化还原开关的作用。
Science. 2017 Feb 24;355(6327). doi: 10.1126/science.aag1789.
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Elaborated Action of the Human Primosome.人类引发体的精细作用
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Mechanism of Concerted RNA-DNA Primer Synthesis by the Human Primosome.人类引发体协同进行RNA-DNA引物合成的机制
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Crystal structure of the C-terminal domain of human DNA primase large subunit: implications for the mechanism of the primase-polymerase α switch.人 DNA 引发酶大亚基 C 端结构域的晶体结构：对引发酶-聚合酶 α 转换机制的影响。
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Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase.从人源 DNA 引发酶的 4Fe-4S 簇结构域的结构和功能相互作用看真核生物 DNA 引发。
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