Structural analysis of human ARS2 as a platform for co-transcriptional RNA sorting
| العنوان: | Structural analysis of human ARS2 as a platform for co-transcriptional RNA sorting |
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| المؤلفون: | Stephen Cusack, Max H. Nanao, Mandy Rettel, Frank Stein, Wiebke Manuela Schulze |
| المصدر: | Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018) 'Nature Communications ', vol: 9, pages: 1701-1-1701-15 (2018) Nature Communications |
| بيانات النشر: | Nature Publishing Group, 2018. |
| سنة النشر: | 2018 |
| مصطلحات موضوعية: | 0301 basic medicine, Science, Protein domain, General Physics and Astronomy, RNA polymerase II, RNA-binding protein, Interactome, General Biochemistry, Genetics and Molecular Biology, Article, 03 medical and health sciences, 0302 clinical medicine, Transcription (biology), parasitic diseases, lcsh:Science, Messenger RNA, Multidisciplinary, biology, Chemistry, RNA, General Chemistry, 3. Good health, Cell biology, 030104 developmental biology, biology.protein, lcsh:Q, 030217 neurology & neurosurgery, Small nuclear RNA |
| الوصف: | ARS2 is a highly conserved metazoan protein involved in numerous aspects of nuclear RNA metabolism. As a direct partner of the nuclear cap-binding complex (CBC), it mediates interactions with diverse RNA processing and transport machineries in a transcript-dependent manner. Here, we present the human ARS2 crystal structure, which exhibits similarities and metazoan-specific differences to the plant homologue SERRATE, most notably an additional RRM domain. We present biochemical, biophysical and cellular interactome data comparing wild type and mutant ARS2 that identify regions critical for interactions with FLASH (involved in histone mRNA biogenesis), NCBP3 (a putative cap-binding protein involved in mRNA export) and single-stranded RNA. We show that FLASH and NCBP3 have overlapping binding sites on ARS2 and that CBC–ARS2–NCBP3 form a ternary complex that is mutually exclusive with CBC–ARS–PHAX (involved in snRNA export). Our results support that mutually exclusive higher-order CBC–ARS2 complexes are critical in determining Pol II transcript fate. Arsenic resistance protein 2 (ARS2) plays an important role in nuclear RNA metabolism and interacts with the nuclear cap-binding complex (CBC). Here the authors present the human ARS2 structure and identify regions important for its interactions with binding partners supporting that mutually exclusive higher order CBC-ARS2 complexes are formed. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 2041-1723 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7162a002b589ea92202a5cb9abbf8bacTest http://link.springer.com/article/10.1038/s41467-018-04142-7Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....7162a002b589ea92202a5cb9abbf8bac |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 20411723 |
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