Structures to complement the archaeo-eukaryotic primases catalytic cycle description: What's next?
Structures to complement the archaeo-eukaryotic primases catalytic cycle description: What's next?
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DOI：
10.1016/j.csbj.2015.04.006
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发表时间：
2015
影响因子：
6
通讯作者：
Lipps G
中科院分区：
文献类型：
--
作者：
Boudet J;Devillier JC;Allain FH;Lipps G
DNA复制是遗传信息从亲本细胞转移到子细胞的关键阶段。这种机制涉及多种蛋白质，其中一个关键因素是引发酶。引物酶是单链DNA依赖性RNA聚合酶。在前导链上，它们合成引物一次，允许DNA延伸，而在滞后链上重复产生引物（冈崎片段）。引物酶具有产生第一个磷酸二酯键的独特能力，从而产生二核苷酸，该二核苷酸最初被引物酶延长，然后被DNA聚合酶延长。在过去的几十年里，人们已经研究了引发酶的活性，但解释一些独特特征的详细分子步骤仍然不清楚。高分辨率的结构的自由和绑定引发酶域带来了显着的见解在理解引发酶反应周期。在这里，我们给出了一个简短的回顾结构的工作进行了考古真核引发酶领域，我们强调失踪的“图片”的酶的活性形式是主要的利益。我们组织了我们的分析方面的进展，通过催化途径。
DNA replication is a crucial stage in the transfer of genetic information from parent to daughter cells. This mechanism involves multiple proteins with one key player being the primase. Primases are single-stranded DNA dependent RNA polymerases. On the leading strand, they synthesize the primer once allowing DNA elongation while on the lagging strand primers are generated repeatedly (Okazaki fragments). Primases have the unique ability to create the first phosphodiester bond yielding a dinucleotide which is initially elongated by primases and then by DNA polymerases. Primase activity has been studied in the last decades but the detailed molecular steps explaining some unique features remain unclear. High-resolution structures of free and bound primases domains have brought significant insights in the understanding of the primase reaction cycle. Here, we give a short review of the structural work conducted in the field of archaeo-eukaryotic primases and we underline the missing “pictures” of the active forms of the enzyme which are of major interest. We organized our analysis with respect to the progression through the catalytic pathway.