RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 αβγ for its activity

• DOI: 10.1073/pnas.95.4.1449
• Publication Date: 2002-07-26T14:42:40Z
• Authors: Tapas Das; Manjula Mathur; Ashim K. Gupta; George M. C. Janssen; Amiya K. Banerjee
• Keywords: RNA polymerase I; Transcription; RNA polymerase II; Elongation factor

An RNA-dependent RNA polymerase is packaged within the virions of purified vesicular stomatitis virus, a nonsegmented negative-strand which carries out transcription genome into mRNAs both in vitro and vivo . The composed two virally encoded polypeptides: large protein L (240 kDa) phosphoprotein P (29 kDa). Recently, we obtained biologically active from insect cells following infection by recombinant baculovirus expressing gene. During purification Sf21 cells, addition to an fraction inactive that required uninfected cell extract restore its activity. cellular factors have now been purified, characterized, shown be β γ subunits synthesis elongation factor EF-1. We also demonstrate α subunit EF-1 remains tightly bound βγ associate with L(α) complex. Further revealed complex partially significantly stimulated cells. A putative inhibitor(s) appears co-elute blocked package all three These findings striking similarity Qβ phage, associates bacterial homologue for replicase function, implicating possible evolutionary relationship between these host proteins viruses.