tetano
Editor, Senior Moderator
J Biol Chem. 2014 Jun 2. pii: jbc.M114.569178. [Epub ahead of print]
The nuclear export protein of H5N1 influenza A viruses recruits M1 to the viral ribonucleoprotein to mediate nuclear export.
Brunotte L1, Flies J1, Bolte H1, Reuther P1, Vreede F2, Schwemmle M3.
Author information
Abstract
In influenza A virus infected cells, replication and transcription of the viral genome occurs in the nucleus. In order to be packaged into viral particles at the plasma membrane, encapsidated viral genomes must be exported from the nucleus. Intriguingly, the nuclear export protein NEP is involved in both processes. While NEP stimulates viral RNA synthesis by binding to the viral polymerase, its function during nuclear export implicates interaction with vRNP-associated M1. The observation that both interactions are mediated by the C-terminal moiety of NEP raised the question whether these two features of NEP are functionally linked. Here, we provide evidence that the interaction between M1 and the vRNP depends on the NEP C-terminus and its polymerase activity-enhancing property for nuclear export of vRNPs. This suggests that these features of NEP are functionally linked. Furthermore, our data suggest that the N-terminal domain of NEP interferes with the stability of the vRNP/M1/NEP nuclear export complex, probably mediated by its highly flexible intramolecular interaction with the NEP C-terminus. Based on our data, we propose a new model for the assembly of the nuclear export complex of Influenza A virus RNPs.
Copyright ? 2014, The American Society for Biochemistry and Molecular Biology.
KEYWORDS:
influenza virus; protein export; ribonuclear protein (RNP); viral polymerase; viral protein
PMID:
24891509
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24891509
The nuclear export protein of H5N1 influenza A viruses recruits M1 to the viral ribonucleoprotein to mediate nuclear export.
Brunotte L1, Flies J1, Bolte H1, Reuther P1, Vreede F2, Schwemmle M3.
Author information
Abstract
In influenza A virus infected cells, replication and transcription of the viral genome occurs in the nucleus. In order to be packaged into viral particles at the plasma membrane, encapsidated viral genomes must be exported from the nucleus. Intriguingly, the nuclear export protein NEP is involved in both processes. While NEP stimulates viral RNA synthesis by binding to the viral polymerase, its function during nuclear export implicates interaction with vRNP-associated M1. The observation that both interactions are mediated by the C-terminal moiety of NEP raised the question whether these two features of NEP are functionally linked. Here, we provide evidence that the interaction between M1 and the vRNP depends on the NEP C-terminus and its polymerase activity-enhancing property for nuclear export of vRNPs. This suggests that these features of NEP are functionally linked. Furthermore, our data suggest that the N-terminal domain of NEP interferes with the stability of the vRNP/M1/NEP nuclear export complex, probably mediated by its highly flexible intramolecular interaction with the NEP C-terminus. Based on our data, we propose a new model for the assembly of the nuclear export complex of Influenza A virus RNPs.
Copyright ? 2014, The American Society for Biochemistry and Molecular Biology.
KEYWORDS:
influenza virus; protein export; ribonuclear protein (RNP); viral polymerase; viral protein
PMID:
24891509
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24891509