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 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.
Mesh Terms:
Alcaligenes, Amino Acid Sequence, Animals, Brain, Cattle, Chromatography, Affinity, Chromatography, Ion Exchange, Endopeptidases, Gene Expression Regulation, Viral, Glycolysis, Humans, Kinetics, Mice, Molecular Sequence Data, Peptide Fragments, Phosphoglycerate Kinase, Phosphopyruvate Hydratase, RNA, Messenger, RNA, Viral, Recombinant Proteins, Respirovirus, Sequence Alignment, Sequence Homology, Amino Acid, Transcription, Genetic, Tubulin
Biochem Biophys Res Commun
Date: Jul. 13, 2001
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