The C-terminal extension of human RTEL1, mutated in Hoyeraal-Hreidarsson syndrome, contains Harmonin-N-like domains
| Autor: | Michael Schertzer, Isabelle Callebaut, Patrick Revy, Guilhem Faure, Arturo Londoño-Vallejo |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Genetics
0303 health sciences biology Sequence analysis DNA repair 030302 biochemistry & molecular biology Helicase Hoyeraal-Hreidarsson syndrome medicine.disease Biochemistry Telomere 03 medical and health sciences Germline mutation Structural Biology biology.protein medicine Molecular Biology Function (biology) Dyskeratosis congenita 030304 developmental biology |
| Zdroj: | Proteins: Structure, Function, and Bioinformatics. 82:897-903 |
| ISSN: | 0887-3585 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text