Faure Guilhem, Revy Patrick, Schertzer Michael, Londono-Vallejo Arturo, Callebaut Isabelle
CNRS, UPMC University Paris 6, IMPMC, UMR7590-IUC, F-75005, Paris, France.
Proteins. 2014 Jun;82(6):897-903. doi: 10.1002/prot.24438. Epub 2013 Nov 22.
Several studies have recently shown that germline mutations in RTEL1, an essential DNA helicase involved in telomere regulation and DNA repair, cause Hoyeraal-Hreidarsson syndrome (HHS), a severe form of dyskeratosis congenita. Using original new softwares, facilitating the delineation of the different domains of the protein and the identification of remote relationships for orphan domains, we outline here that the C-terminal extension of RTEL1, downstream of its catalytic domain and including several HHS-associated mutations, contains a yet unidentified tandem of harmonin-N-like domains, which may serve as a hub for partner interaction. This finding highlights the potential critical role of this region for the function of RTEL1 and gives insights into the impact that the identified mutations would have on the structure and function of these domains.
最近的几项研究表明,RTEL1(一种参与端粒调控和DNA修复的重要DNA解旋酶)中的种系突变会导致霍耶拉尔-赫雷达尔松综合征(HHS),这是先天性角化不良的一种严重形式。我们使用了新的原创软件,这些软件有助于描绘该蛋白质的不同结构域,并识别孤儿结构域的远程关系。在此我们概述,RTEL1的C末端延伸区域位于其催化结构域下游,包含几个与HHS相关的突变,其中含有一个尚未确定的类harmonin-N串联结构域,它可能作为伙伴相互作用的枢纽。这一发现突出了该区域对RTEL1功能的潜在关键作用,并深入了解了已识别的突变对这些结构域的结构和功能可能产生的影响。