人类HLTF新型DNA结合结构域的晶体学研究，该结构域参与模板转换途径以避免DNA损伤引起的复制停滞。
Crystallographic study of a novel DNA-binding domain of human HLTF involved in the template-switching pathway to avoid the replication arrest caused by DNA damage.
作者信息
Ikegaya Yuzu, Hara Kodai, Hishiki Asami, Yokoyama Hideshi, Hashimoto Hiroshi
机构信息
School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka, Shizuoka 422-8002, Japan.
出版信息
Acta Crystallogr F Struct Biol Commun. 2015 Jun;71(Pt 6):668-70. doi: 10.1107/S2053230X15005907. Epub 2015 May 20.
Abstract
HLTF is a pivotal protein in the template-switching pathway that allows DNA synthesis to continue even in the presence of DNA damage by utilizing a newly synthesized undamaged strand as a template. HLTF has a novel DNA-binding domain termed HIRAN that has been recently found in various proteins, although its detailed function remains unclear. In this study, the HIRAN domain of human HLTF was successfully crystallized. The crystals belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 130.0, c = 150.1 Å.
摘要
HLTF是模板转换途径中的一种关键蛋白，它通过利用新合成的未受损链作为模板，使DNA合成即使在存在DNA损伤的情况下也能继续进行。HLTF具有一个名为HIRAN的新型DNA结合结构域，该结构域最近在多种蛋白质中被发现，但其详细功能仍不清楚。在本研究中，人HLTF的HIRAN结构域成功结晶。晶体属于空间群P4(1)2(1)2或P4(3)2(1)2，晶胞参数a = b = 130.0，c = 150.1 Å。
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