Human papillomavirus type 6 E7 protein is a substrate in vitro of protein kinase C.
The E7 proteins of 'low-risk' and 'high-risk' human papillomaviruses (HPV) are phosphorylated by casein kinase II. In this study, we report that the 'low-risk' HPV 6 E7 protein, but not the 'high-risk' HPV 16 E7 protein, can be phosphorylated in vitro on threonine at amino acid position 7 by protein kinase C. This is the first example of a qualitative biochemical difference between the HPV 6 E7 and HPV 16 E7 proteins.
Armstrong
D J
DJ
Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis 46202-5120, USA.
Roman
A
A
D000595:Amino Acid Sequence; D001483:Base Sequence; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009856:Oncogene Proteins, Viral / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D027383:Papillomaviridae; D050725:Papillomavirus E7 Proteins; D010766:Phosphorylation; D010769:Phosphothreonine / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017385:Sequence Homology; D013379:Substrate Specificity
D009856:Oncogene Proteins, Viral; D050725:Papillomavirus E7 Proteins; D011993:Recombinant Fusion Proteins; C059731:oncogene protein E7, Human papillomavirus type 16; C062495:oncogene protein E7, Human papillomavirus type 6; D010769:Phosphothreonine; D011493:Protein Kinase C