A Complex of the Bacteriophage T7 Primase-Helicase and DNA Polymerase Directs Primer Utilization
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference55 articles.
1. Bacteriophage T7: Minimal requirements for the replication of a duplex DNA molecule
2. Coordinated Leading and Lagging Strand DNA Synthesis on a Minicircular Template
3. Interactions of the DNA polymerase and gene 4 protein of bacteriophage T7. Protein-protein and protein-DNA interactions involved in RNA-primed DNA synthesis.
4. The Acidic Carboxyl Terminus of the Bacteriophage T7 Gene 4 Helicase/Primase Interacts with T7 DNA Polymerase
5. Acidic carboxyl-terminal domain of gene 2.5 protein of bacteriophage T7 is essential for protein-protein interactions.
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1. The plant organellar primase-helicase directs template recognition and primosome assembly via its zinc finger domain;BMC Plant Biology;2023-10-06
2. Residues located in the primase domain of the bacteriophage T7 primase-helicase are essential for loading the hexameric complex onto DNA;Journal of Biological Chemistry;2022-06
3. Structure of an open conformation of T7 DNA polymerase reveals novel structural features regulating primer-template stabilization at the polymerization active site;Biochemical Journal;2021-07-16
4. Metabolic cofactors NADH and FAD act as non-canonical initiating substrates for a primase and affect replication primer processing in vitro;Nucleic Acids Research;2020-05-28
5. Genome characterization of novel lytic Myoviridae bacteriophage ϕVP-1 enhances its applicability against MDR-biofilm-forming Vibrio parahaemolyticus;Archives of Virology;2019-12-21
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