PMID:21606333

Citation	Zhang, H, Lee, SJ, Zhu, B, Tran, NQ, Tabor, S and Richardson, CC (2011) Helicase-DNA polymerase interaction is critical to initiate leading-strand DNA synthesis. Proc. Natl. Acad. Sci. U.S.A. 108:9372-7
Abstract	Interactions between gene 4 helicase and gene 5 DNA polymerase (gp5) are crucial for leading-strand DNA synthesis mediated by the replisome of bacteriophage T7. Interactions between the two proteins that assure high processivity are known but the interactions essential to initiate the leading-strand DNA synthesis remain unidentified. Replacement of solution-exposed basic residues (K587, K589, R590, and R591) located on the front surface of gp5 with neutral asparagines abolishes the ability of gp5 and the helicase to mediate strand-displacement synthesis. This front basic patch in gp5 contributes to physical interactions with the acidic C-terminal tail of the helicase. Nonetheless, the altered polymerase is able to replace gp5 and continue ongoing strand-displacement synthesis. The results suggest that the interaction between the C-terminal tail of the helicase and the basic patch of gp5 is critical for initiation of strand-displacement synthesis. Multiple interactions of T7 DNA polymerase and helicase coordinate replisome movement.
Links	PubMed PMC3111293 Online version:10.1073/pnas.1106678108
Keywords	Bacteriophage T7/genetics; Bacteriophage T7/metabolism; Binding Sites/genetics; DNA Helicases/chemistry; DNA Helicases/genetics; DNA Helicases/metabolism; DNA Replication; DNA, Single-Stranded/chemistry; DNA, Single-Stranded/genetics; DNA, Single-Stranded/metabolism; DNA, Viral/chemistry; DNA, Viral/genetics; DNA, Viral/metabolism; DNA-Directed DNA Polymerase/chemistry; DNA-Directed DNA Polymerase/genetics; DNA-Directed DNA Polymerase/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli/virology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Models, Molecular; Mutation; Nucleic Acid Conformation; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Surface Plasmon Resonance; Thioredoxins/chemistry; Thioredoxins/genetics; Thioredoxins/metabolism; Viral Proteins/chemistry; Viral Proteins/genetics; Viral Proteins/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BPT7:DPOL		GO:0090592: DNA synthesis involved in DNA replication	ECO:0000315:		P		Figure 2 compared the activities of both gp5/trx and its mutated form Gp5-Fbpneu/trx in the presence of gp4 by looking at how much nucleotide (dTMP) had been incorporated in a sample of dsDNA . According to the paper and from the results, Gp5-Fbpneu/trx did not mediate the synthesis in the presence of gp4 over a large range of concentrations of gp5/trx and gp4. This means that a mutated gp5 would result in disrupted DNA synthesis in the presence of gp4 as compared to a normal version of gp5, showing its critical function for DNA replication.	complete CACAO 13104

References

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