Serine/arginine-rich protein 30c activates human papillomavirus type 16 L1 mRNA expression via a bimodal mechanism
2011 (English)In: Journal of General Virology, ISSN 0022-1317, E-ISSN 1465-2099, Vol. 92, no 10, 2411-2421 p.Article in journal (Refereed) Published
Two splice sites on the human papillomavirus type 16 (HPV-16) genome are used exclusively by the late capsid protein L1 mRNAs: SD3632 and SA5639. These splice sites are suppressed in mitotic cells. This study showed that serine/arginine-rich protein 30c (SRp30c), also named SFRS9, activated both SD3632 and SA5639 and induced production of L1 mRNA. Activation of HPV-16 L1 mRNA splicing by SRp30c required an intact arginine/serine-repeat (RS) domain of SRp30c. In addition to this effect, SRp30c could enhance L1 mRNA production indirectly by inhibiting the early 3′-splice site SA3358, which competed with the late 3′-splice site SA5639. SRp30c bound directly to sequences downstream of SA3358, suggesting that SRp30c inhibited the enhancer at SA3358 and caused a redirection of splicing to the late 3′-splice site SA5639. This inhibitory effect of SRp30c was independent of its RS domain. These results suggest that SRp30c can activate HPV-16 L1 mRNA expression via a bimodal mechanism: directly by stimulating splicing to late splice sites and indirectly by inhibiting competing early splice sites.
Place, publisher, year, edition, pages
2011. Vol. 92, no 10, 2411-2421 p.
HPV-16, splicing, SR-proteins, SRp30c, polyadenylation
Microbiology in the medical area
Research subject Medical Virology
IdentifiersURN: urn:nbn:se:uu:diva-150707DOI: 10.1099/vir.0.033183-0ISI: 000295856000022OAI: oai:DiVA.org:uu-150707DiVA: diva2:408525