Purification and DNA-binding properties of human papillomavirus type 16 E6 protein expressed in Escherichia coli.
Unfused human papillomavirus type 16 (HPV 16) E6 protein was expressed in Escherichia coli using a lambda PL promoter system. The protein was isolated from the cells as inclusion bodies, extracted by 6 M guanidine-HCl, and purified by chromatography. The purified protein had high affinity to DNA and was demonstrated for the first time to bind to a specific sequence within the long control region of HPV 16.
Imai
Y
Y
National Cancer Center Research Institute, Tokyo, Japan.
Tsunokawa
Y
Y
Sugimura
T
T
Terada
M
M
D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000302:isolation & purification*; D004742:Enhancer Elements, Genetic; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005814:Genes, Viral; D005822:Genetic Vectors; D015151:Immunoblotting; D007700:Kinetics; D009856:Oncogene Proteins, Viral / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D027383:Papillomaviridae / Q000235:genetics* / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification / Q000378:metabolism; D015183:Restriction Mapping; D015678:Viral Structural Proteins / Q000235:genetics
D004268:DNA-Binding Proteins; D009856:Oncogene Proteins, Viral; D011993:Recombinant Fusion Proteins; D015678:Viral Structural Proteins; C059269:protein E6, Bovine papillomavirus