Lo, Chen-Yu; Gao, Yang published the artcile< DNA Polymerase-Parental DNA Interaction Is Essential for Helicase-Polymerase Coupling during Bacteriophage T7 DNA Replication>, Reference of 452-06-2, the main research area is bacteriophage T7 DNA replication polymerase helicase coupling; DNA replication; bacteriophage T7; helicase; polymerase.
DNA helicase and polymerase work cooperatively at the replication fork to perform leading-strand DNA synthesis. It was believed that the helicase migrates to the forefront of the replication fork where it unwinds the duplex to provide templates for DNA polymerases. However, the mol. basis of the helicase-polymerase coupling is not fully understood. The recently elucidated T7 replisome structure suggests that the helicase and polymerase sandwich parental DNA and each enzyme pulls a daughter strand in opposite directions. Interestingly, the T7 polymerase, but not the helicase, carries the parental DNA with a pos. charged cleft and stacks at the fork opening using a β-hairpin loop. Here, we created and characterized T7 polymerases each with a perturbed β-hairpin loop and pos. charged cleft. Mutations on both structural elements significantly reduced the strand-displacement synthesis by T7 polymerase but had only a minor effect on DNA synthesis performed against a linear DNA substrate. Moreover, the aforementioned mutations eliminated synergistic helicase-polymerase binding and unwinding at the DNA fork and processive fork progressions. Thus, our data suggested that T7 polymerase plays a dominant role in helicase-polymerase coupling and replisome progression.
International Journal of Molecular Sciences published new progress about Coliphage T7. 452-06-2 belongs to class imidazoles-derivatives, and the molecular formula is C5H5N5, Reference of 452-06-2.
Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem