Publications by authors named "Geoff G Kneale"
Article Synopsis
- The C terminus of the herpes simplex virus type 1 origin-binding protein, UL9ct, interacts with the viral single-stranded DNA-binding protein ICP8, specifically a mutant version called ICP8DeltaC.
- Research using various techniques, including small angle x-ray scattering, reveals the structures of UL9ct alone and in complex with ICP8DeltaC and DNA, highlighting a binding stoichiometry of 2:1 for UL9ct and a 15-mer DNA.
- The study suggests a two-step binding process for UL9ct to DNA and describes a model where UL9ct's conformational change allows for the recruitment of the UL9-ICP8 complex, forming a larger assembly on the origin of replication
Histidine (His) tags are one of the most popular fusion tags for the isolation of proteins via metal affinity chromatography. The fusion tag is routinely left attached to the protein when carrying out experiments, with the assumption that the addition has no effect on structure or function. In the present study, we have prepared four proteins of the gene regulatory protein AreA from Aspergillus nidulans for crystallization experiments: a 91-amino acid peptide encompassing the minimal DNA-binding region, both with and without the His-tag (HZFB and ZFB, respectively), and a 155-amino acid protein previously proposed to be the entire DNA-binding domain for AreA, both with and without the His-tag (HG1b and G1b, respectively).
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