tetano
Editor, Senior Moderator
FEBS Lett. 2013 May 28. pii: S0014-5793(13)00383-9. doi: 10.1016/j.febslet.2013.05.029. [Epub ahead of print]
Non-structural protein 1 of influenza viruses inhibits rapid mRNA degradation mediated by double-stranded RNA-binding protein, staufen1.
Cho H, Ahn SH, Kim KM, Kim YK.
Source
School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
Abstract
Although non-structural protein 1 (NS1) of influenza viruses is not essential for virulence, this protein is involved in host-virus interactions, viral replication, and translation. In particular, NS1 is known to interact with the host protein, staufen1 (Stau1). This interaction is important for efficient viral replication. However, the underlying molecular mechanism by which NS1 influences the viral life cycle remains obscure. Here, we show using immunoprecipitation and artificial tethering that the N-terminus of NS1, NS1(1-73), interacts with Stau1, blocks the Stau1-Upf1 interaction, and consequently inhibits the efficiency of Stau1-mediated mRNA decay (SMD), but not non-sense-mediated mRNA decay (NMD). The regulation of SMD efficiency by NS1 may contribute to building a more favorable cellular environment for viral replication. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: STAU1-55physically interacts with UPF1 by anti tagcoimmunoprecipitation (View interaction) NS1physically interacts with STAU1-55 by anti tagcoimmunoprecipitation (View interaction).
Copyright ? 2013. Published by Elsevier B.V.
PMID:
23722113
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23722113
Non-structural protein 1 of influenza viruses inhibits rapid mRNA degradation mediated by double-stranded RNA-binding protein, staufen1.
Cho H, Ahn SH, Kim KM, Kim YK.
Source
School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
Abstract
Although non-structural protein 1 (NS1) of influenza viruses is not essential for virulence, this protein is involved in host-virus interactions, viral replication, and translation. In particular, NS1 is known to interact with the host protein, staufen1 (Stau1). This interaction is important for efficient viral replication. However, the underlying molecular mechanism by which NS1 influences the viral life cycle remains obscure. Here, we show using immunoprecipitation and artificial tethering that the N-terminus of NS1, NS1(1-73), interacts with Stau1, blocks the Stau1-Upf1 interaction, and consequently inhibits the efficiency of Stau1-mediated mRNA decay (SMD), but not non-sense-mediated mRNA decay (NMD). The regulation of SMD efficiency by NS1 may contribute to building a more favorable cellular environment for viral replication. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: STAU1-55physically interacts with UPF1 by anti tagcoimmunoprecipitation (View interaction) NS1physically interacts with STAU1-55 by anti tagcoimmunoprecipitation (View interaction).
Copyright ? 2013. Published by Elsevier B.V.
PMID:
23722113
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23722113