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Updated: Aug 8, 2026

Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins
Published on: February 25, 2017
The phage N4 virion RNA polymerase catalytic domain is related to single-subunit RNA polymerases
K M Kazmierczak1, E K Davydova, A A Mustaev
1Department of Molecular Genetics and Cell Biology, The University of Chicago, 920 East 58th Street, IL 60637, USA.
Abstract:
In vitro, bacteriophage N4 virion RNA polymerase (vRNAP) recognizes in vivo sites of transcription initiation on single-stranded templates. N4 vRNAP promoters are comprised of a hairpin structure and conserved sequences. Here, we show that vRNAP consists of a single 3500 amino acid polypeptide, and we define and characterize a transcriptionally active 1106 amino acid domain (mini-vRNAP). Biochemical and genetic characterization of this domain indicates that, despite its peculiar promoter specificity and lack of extensive sequence similarity to other DNA-dependent RNA polymerases, mini-vRNAP is related to the family of T7-like RNA polymerases.
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