Enolase, a cellular glycolytic enzyme, is required for efficient transcription of Sendai virus genome

Cellular proteins (host factors) may play key roles in transcription of Sen dai virus (SeV) genome. We have previously shown that the host factor activ ity, which stimulates in vitro mRNA synthesis of SeV, from bovine brain com prises at least three complementary factors, and two of them were identifie d as tubulin and phosphoglycerate kinase (PGK), Here the third host factor activity was further resolved into two complementary factors, and one of th em was purified to an almost single polypeptide chain with an apparent 2M, of 52,000 (p52) and was identified as a glycolytic enzyme, enolase, Recombi nant human alpha -enolase, as did p52, acted synergistically with other thr ee host factors to stimulate SeV mRNA synthesis. West-Western blot analysis demonstrated that tubulin specifically binds enolase as well as PGK, sugge sting that these two glycolytic enzymes regulate SeV transcription through their interactions with tubulin. (C) 2001 Academic Press.