Ogino T, Yamadera T, Nonaka T, Imajoh-Ohmi S, Mizumoto K
Department of Biochemistry, School of Pharmaceutical Sciences, Kitasato University, Shirokane, Minato-ku, Tokyo 108-8641, Japan.
Biochem Biophys Res Commun. 2001 Jul 13;285(2):447-55. doi: 10.1006/bbrc.2001.5160.
Cellular proteins (host factors) may play key roles in transcription of Sendai virus (SeV) genome. We have previously shown that the host factor activity, which stimulates in vitro mRNA synthesis of SeV, from bovine brain comprises at least three complementary factors, and two of them were identified as tubulin and phosphoglycerate kinase (PGK). Here the third host factor activity was further resolved into two complementary factors, and one of them was purified to an almost single polypeptide chain with an apparent M(r) of 52,000 (p52) and was identified as a glycolytic enzyme, enolase. Recombinant human alpha-enolase, as did p52, acted synergistically with other three host factors to stimulate SeV mRNA synthesis. West-Western blot analysis demonstrated that tubulin specifically binds enolase as well as PGK, suggesting that these two glycolytic enzymes regulate SeV transcription through their interactions with tubulin.
