Identification of a domain of the herpes simplex virus trans-activator Vmw65 required for protein-DNA complex formation through the use of protein A fusion proteins.
In order to identify structural domains of the herpes simplex virus trans-activator Vmw65 required for protein-DNA complex formation, subfragments of Vmw65 were expressed in Escherichia coli as fusion polypeptides with protein A of Staphylococcus aureus, and the purified hybrids were used in a band shift assay. The results indicate that a region near the amino terminus of Vmw65 between amino acids 141 and 185 is necessary for complex formation.
Werstuck
G
G
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
Capone
J P
JP
D001483:Base Sequence; D003001:Cloning, Molecular; D004279:DNA, Viral / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D005814:Genes, Viral; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D010957:Plasmids; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D018139:Simplexvirus / Q000235:genetics*; D013205:Staphylococcal Protein A / Q000235:genetics* / Q000378:metabolism; D015534:Trans-Activators / Q000302:isolation & purification / Q000378:metabolism*
D004279:DNA, Viral; D015345:Oligonucleotide Probes; D011993:Recombinant Fusion Proteins; D013205:Staphylococcal Protein A; D015534:Trans-Activators