Academic Journal
Ribosomal protein S19-binding domain provides insights into hantavirus nucleocapsid protein-mediated translation initiation mechanism
| العنوان: | Ribosomal protein S19-binding domain provides insights into hantavirus nucleocapsid protein-mediated translation initiation mechanism |
|---|---|
| المؤلفون: | Ganaie, Safder S., Haque, Absarul, Cheng, Erdong, Bonny, Tania S., Salim, Nilshad N., Mir, Mohammad A. |
| المصدر: | Biochemical Journal ; volume 464, issue 1, page 109-121 ; ISSN 0264-6021 1470-8728 |
| بيانات النشر: | Portland Press Ltd. |
| سنة النشر: | 2014 |
| الوصف: | The hantaviral zoonotic diseases pose a significant threat to human health due to the lack of potential antiviral therapeutics or a vaccine against hantaviruses. N (Sin Nombre hantavirus nucleocapsid protein) augments mRNA translation. N binds to both the mRNA 5′ cap and 40S ribosomal subunit via RPS19 (ribosomal protein S19). N with the assistance of the viral mRNA 5′-UTR preferentially favours the translation of a downstream ORF. We identified and characterized the RPS19-binding domain at the N-terminus of N. Its deletion did not influence the secondary structure, but affected the conformation of trimeric N molecules. The N variant lacking the RPS19-binding region was able to bind both the mRNA 5′ cap and panhandle-like structure, formed by the termini of viral genomic RNA. In addition, the N variant formed stable trimers similar to wild-type N. Use of this variant in multiple experiments provided insights into the mechanism of ribosome loading during N-mediated translation strategy. The present study suggests that N molecules individually associated with the mRNA 5′ cap and RPS19 of the 40S ribosomal subunit undergo N–N interaction to facilitate the engagement of N-associated ribosomes at the mRNA 5′ cap. This has revealed new targets for therapeutic intervention of hantavirus infection. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| DOI: | 10.1042/bj20140449 |
| الاتاحة: | http://dx.doi.org/10.1042/bj20140449 https://portlandpress.com/biochemj/article-pdf/464/1/109/681573/bj4640109.pdf |
| رقم الانضمام: | edsbas.F45F50C |
| قاعدة البيانات: | BASE |
كن أول من يترك تعليقا!