Charles C. Richardson

Lagging strand synthesis in coordinated DNA synthesis by bacteriophage t7 replication proteins.

Interaction of adjacent primase domains within the hexameric gene 4 helicase-primase of bacteriophage T7.

Essential amino acid residues in the single-stranded DNA-binding protein of bacteriophage T7. Identification of the dimer interface.

The DNA binding domain of the gene 2.5 single-stranded DNA-binding protein of bacteriophage T7.

A covalent linkage between the gene 5 DNA polymerase of bacteriophage T7 and Escherichia coli thioredoxin, the processivity factor: fate of thioredoxin during DNA synthesis.

A single-stranded DNA-binding protein of bacteriophage T7 defective in DNA annealing.

The carboxyl-terminal domain of bacteriophage T7 single-stranded DNA-binding protein modulates DNA binding and interaction with T7 DNA polymerase.

Modular architecture of the bacteriophage T7 primase couples RNA primer synthesis to DNA synthesis.

Single-molecule kinetics of lambda exonuclease reveal base dependence and dynamic disorder.

Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli.

Effect of single-stranded DNA-binding proteins on the helicase and primase activities of the bacteriophage T7 gene 4 protein.

The linker region between the helicase and primase domains of the gene 4 protein of bacteriophage T7. Role in helicase conformation and activity.

The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling.

A unique region in bacteriophage t7 DNA polymerase important for exonucleolytic hydrolysis of DNA.

The highly processive DNA polymerase of bacteriophage T5. Role of the unique N and C termini.

Crystal structures of 2-acetylaminofluorene and 2-aminofluorene in complex with T7 DNA polymerase reveal mechanisms of mutagenesis.

A unique loop in T7 DNA polymerase mediates the binding of helicase-primase, DNA binding protein, and processivity factor.

Acidic residues in the nucleotide-binding site of the bacteriophage T7 DNA primase.

DNA-induced switch from independent to sequential dTTP hydrolysis in the bacteriophage T7 DNA helicase.

DNA primase acts as a molecular brake in DNA replication.

Primer initiation and extension by T7 DNA primase.

Oligomeric states of bacteriophage T7 gene 4 primase/helicase.

The C-terminal residues of bacteriophage T7 gene 4 helicase-primase coordinate helicase and DNA polymerase activities.

Essential residues in the C terminus of the bacteriophage T7 gene 2.5 single-stranded DNA-binding protein.

Single molecule force spectroscopy of salt-dependent bacteriophage T7 gene 2.5 protein binding to single-stranded DNA.

Genomewide screens for Escherichia coli genes affecting growth of T7 bacteriophage.

Exchange of DNA polymerases at the replication fork of bacteriophage T7.

Dynamic DNA helicase-DNA polymerase interactions assure processive replication fork movement.

Inadequate inhibition of host RNA polymerase restricts T7 bacteriophage growth on hosts overexpressing udk.

Acidic C-terminal tail of the ssDNA-binding protein of bacteriophage T7 and ssDNA compete for the same binding surface.

Communication between subunits critical to DNA binding by hexameric helicase of bacteriophage T7.

Gene 1.7 of bacteriophage T7 confers sensitivity of phage growth to dideoxythymidine.

Peptide ligands specific to the oxidized form of Escherichia coli thioredoxin.

Interactions of Escherichia coli thioredoxin, the processivity factor, with bacteriophage T7 DNA polymerase and helicase.

Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis.

DNA recognition by the DNA primase of bacteriophage T7: a structure-function study of the zinc-binding domain.

Promiscuous usage of nucleotides by the DNA helicase of bacteriophage T7: determinants of nucleotide specificity.

Motors, switches, and contacts in the replisome.

Mutations in the gene 5 DNA polymerase of bacteriophage T7 suppress the dominant lethal phenotype of gene 2.5 ssDNA binding protein lacking the C-terminal phenylalanine.

Rescue of bacteriophage T7 DNA polymerase of low processivity by suppressor mutations affecting gene 3 endonuclease.

An in trans interaction at the interface of the helicase and primase domains of the hexameric gene 4 protein of bacteriophage T7 modulates their activities.

C-terminal phenylalanine of bacteriophage T7 single-stranded DNA-binding protein is essential for strand displacement synthesis by T7 DNA polymerase at a nick in DNA.

Thioredoxin suppresses microscopic hopping of T7 DNA polymerase on duplex DNA.

Mechanism of sequence-specific template binding by the DNA primase of bacteriophage T7.

Residues in the central beta-hairpin of the DNA helicase of bacteriophage T7 are important in DNA unwinding.

Two modes of interaction of the single-stranded DNA-binding protein of bacteriophage T7 with the DNA polymerase-thioredoxin complex.

Direct role for the RNA polymerase domain of T7 primase in primer delivery.

A novel nucleotide kinase encoded by gene 1.7 of bacteriophage T7.

Molecular basis for recognition of nucleoside triphosphate by gene 4 helicase of bacteriophage T7.

Conformational dynamics of bacteriophage T7 DNA polymerase and its processivity factor, Escherichia coli thioredoxin.

Simultaneous single-molecule measurements of phage T7 replisome composition and function reveal the mechanism of polymerase exchange.

The glutamate switch of bacteriophage T7 DNA helicase: role in coupling nucleotide triphosphate (NTP) and DNA binding to NTP hydrolysis.

Helicase-DNA polymerase interaction is critical to initiate leading-strand DNA synthesis.

Pyrovanadolysis, a pyrophosphorolysis-like reaction mediated by pyrovanadate, Mn2+, and DNA polymerase of bacteriophage T7.

Bypass of a nick by the replisome of bacteriophage T7.

Coupling dTTP hydrolysis with DNA unwinding by the DNA helicase of bacteriophage T7.

Choreography of bacteriophage T7 DNA replication.

Essential protein interactions within the replisome regulate DNA replication.