Academic Journal
Translocation portals for the substrates and products of a viral transcription complex: the bluetongue virus core.
| العنوان: | Translocation portals for the substrates and products of a viral transcription complex: the bluetongue virus core. |
|---|---|
| المؤلفون: | Diprose, Jm, Burroughs, Jn, Sutton, Gc, Goldsmith, A., Gouet, P., Malby, R., Overton, I., Zientara, Stéphan, Mertens, Pp, Stuart, Di, Grimes, Jm |
| المساهمون: | Institut de biologie et chimie des protéines Lyon (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS) |
| المصدر: | ISSN: 0261-4189. |
| بيانات النشر: | HAL CCSD EMBO Press |
| سنة النشر: | 2001 |
| المجموعة: | Université de Lyon: HAL |
| مصطلحات موضوعية: | [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology |
| الوصف: | International audience ; The bluetongue virus core is a molecular machine that simultaneously and repeatedly transcribes mRNA from 10 segments of viral double-stranded RNA, packaged in a liquid crystalline array. To determine how the logistical problems of transcription within a sealed shell are solved, core crystals were soaked with various ligands and analysed by X-ray crystallography. Mg(2+) ions produce a slight expansion of the capsid around the 5-fold axes. Oligonucleotide soaks demonstrate that the 5-fold pore, opened up by this expansion, is the exit site for mRNA, whilst nucleotide soaks pinpoint a separate binding site that appears to be a selective channel for the entry and exit of substrates and by-products. Finally, nucleotides also bind to the outer core layer, providing a substrate sink.The bluetongue virus core is a molecular machine that simultaneously and repeatedly transcribes mRNA from 10 segments of viral double-stranded RNA, packaged in a liquid crystalline array. To determine how the logistical problems of transcription within a sealed shell are solved, core crystals were soaked with various ligands and analysed by X-ray crystallography. Mg(2+) ions produce a slight expansion of the capsid around the 5-fold axes. Oligonucleotide soaks demonstrate that the 5-fold pore, opened up by this expansion, is the exit site for mRNA, whilst nucleotide soaks pinpoint a separate binding site that appears to be a selective channel for the entry and exit of substrates and by-products. Finally, nucleotides also bind to the outer core layer, providing a substrate sink. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | info:eu-repo/semantics/altIdentifier/pmid/11742999; hal-00314282; https://hal.science/hal-00314282; PUBMED: 11742999 |
| الاتاحة: | https://hal.science/hal-00314282 |
| رقم الانضمام: | edsbas.2FAD2104 |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |