A novel single-strand specific 3'-5' exonuclease found in the hyperthermophilic archaeon, Pyrococcus furiosus.
A novel single-strand specific 3'-5' exonuclease found in the hyperthermophilic archaeon, Pyrococcus furiosus.
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DOI：
10.1371/journal.pone.0058497
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发表时间：
2013
期刊：
影响因子：
3.7
通讯作者：
Ishino Y
中科院分区：
文献类型：
--
作者：
Tori K;Ishino S;Kiyonari S;Tahara S;Ishino Y
核酸酶在包括复制、修复和重组在内的所有DNA交易中起着重要作用。来自细菌和真核生物的许多不同的核酸酶已经被鉴定和功能表征。然而，我们对来自古生菌（生命的第三领域）的核酸酶的了解仍然有限。我们在嗜热古细菌furiosus中寻找3′-5′外切酶活性，并鉴定出具有目标活性的蛋白。该纯化蛋白由PF2046编码，由229个氨基酸组成，分子量为25,596，具有单链特异性3 ‘ -5 ’外切酶活性。该蛋白被命名为PfuExo I，在溶液中形成稳定的三聚体复合物，并从3 ‘到5 ’方向上每两个核苷酸切除DNA。该蛋白的氨基酸序列仅在热球菌中保守，热球菌是古细菌中Euryarchaeota亚域的超嗜热类之一。新发现的外切酶与任何其他已知功能的蛋白质缺乏相似性，包括迄今报道的3 ‘ -5 ’外切酶。这种新型核酸酶可能作为某些嗜热古菌的特定成员参与了生物体中保守的DNA修复途径。
Nucleases play important roles in all DNA transactions, including replication, repair, and recombination. Many different nucleases from bacterial and eukaryotic organisms have been identified and functionally characterized. However, our knowledge about the nucleases from Archaea, the third domain of life, is still limited. We searched for 3′–5′ exonuclease activity in the hyperthermophilic archaeon, Pyrococcus furiosus, and identified a protein with the target activity. The purified protein, encoded by PF2046, is composed of 229 amino acids with a molecular weight of 25,596, and displayed single-strand specific 3′–5′ exonuclease activity. The protein, designated as PfuExo I, forms a stable trimeric complex in solution and excises the DNA at every two nucleotides from the 3′ to 5′ direction. The amino acid sequence of this protein is conserved only in Thermococci, one of the hyperthermophilic classes in the Euryarchaeota subdomain in Archaea. The newly discovered exonuclease lacks similarity to any other proteins with known function, including hitherto reported 3′–5′ exonucleases. This novel nuclease may be involved in a DNA repair pathway conserved in the living organisms as a specific member for some hyperthermophilic archaea.
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