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首页> 外文期刊>Journal of Molecular Biology >Identification of a Structurally Dynamic Domain for Oligomer Formation in Rootletin
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Identification of a Structurally Dynamic Domain for Oligomer Formation in Rootletin

机译：rootlin中寡聚物形成的结构动态结构域的鉴定

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Rootletin is the main component of the ciliary rootlet and functions as a centriole linker connecting the two mother centrioles. Despite the functional importance of rootletin, the molecular architecture of the rootletin filament and its assembly mechanism are poorly understood. Here, we identify the coiled-coil domain 3 (CCD3) of rootletin as the key domain for its cellular function. The crystal structure of the CCD3(1108-1317) fragment containing 28 heptad repeats and 1 hendecad repeat reveals that it forms a parallel coiled-coil dimer spanning approximately 300 angstrom in length. Crosslinking experiments and biophysical analyses of the minimal functional region of CCD3 (CCD3-6) suggest that CCD3-6 is structurally dynamic and may be important for oligomer formation. We also show that oligomerization-defective CCD3 mutants fail in centrosomal localization and centriole linkage, suggesting that rootletin oligomerization may be important for its function. (C) 2020 The Author(s). Published by Elsevier Ltd.
机译：rootlin是睫状根蛋白的主要成分，并用作连接两个母线摩洛尔的厘氢接头。尽管rootin素的功能性重要性，rootlin灯丝的分子结构及其组装机​​制尚未理解。在这里，我们将rootin素的卷绕式线圈结构域3（CCD3）识别为其蜂窝功能的关键域。含有28个胚A重复的CCD3（1108-1317）片段的晶体结构和1 Hendecad重复揭示了它形成了长度约为300埃的平行卷轴线圈二聚体。 CCD3（CCD3-6）最小官能区域的交联实验和生物物理学分析表明CCD3-6在结构上是动态的，对于低聚物形成可能是重要的。我们还表明，寡聚化缺陷的CCD3突变体在Centomal定位和厘氢键中失败，表明rootlin寡聚化可能对其功能很重要。 （c）2020提交人。 elsevier有限公司出版

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