Journal article

Influenza virus M1 protein binds to RNA through its nuclear localization signal

Elster C, Larsen K, Gagnon J, Ruigrok R, Baudin F ...see all

Journal of General Virology, vol. 78, issue 7 (1997) pp. 1589-1596

  • 38


    Mendeley users who have this article in their library.
  • 65


    Citations of this article.
  • N/A


    ScienceDirect users who have downloaded this article.
Sign in to save reference


The RNA-binding activity of influenza A virus M1 protein was studied by cross-linking the protein to viral RNA followed by sequence analysis of the oligoribonucleotide bound to the protein as well as sequence analysis of the M1 peptide bound to the RNA. M1 was found to bind to RNA without any RNA sequence specificity, as verified in a series of filter-binding experiments using a large variety of nucleic acids including DNA. The peptide sequence that bound to the RNA was the RKLKR nuclear localization signal of M1. Site-specific mutagenesis of recombinant M1 showed that most of the basic residues in that region had to be mutated in order to inhibit RNA-binding. We also constructed an M1 mutant that no longer bound to RNA but which was still able to inhibit the in vitro transcription activity of isolated viral ribonucleoprotein, albeit to a lower extent. Mutation of the zinc-binding sequence had no effect on RNA-binding or transcription-inhibition activity.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Get full text


  • Jean GagnonPAVAL lab, University Grenoble-Alpes

  • Christine Elster

  • Kjeld Larsen

  • Rob W.H. Ruigrok

  • Florence Baudin

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free