title: Human papillomavirus 16 E2 stability and transcriptional activation is enhanced by E1 via a direct protein-protein interaction.
abstract: Human papillomavirus 16 E1 and E2 interact with cellular factors to replicate the viral genome. E2 forms homodimers and binds to 12 bp palindromic sequences adjacent to the viral origin and recruits E1 to the origin. E1 forms a di-hexameric helicase complex that replicates the viral genome. This manuscript demonstrates that E1 stabilises the E2 protein, increasing the half life in both C33a and 293 T cells respectively. This stabilisation requires a direct protein--protein interaction. In addition, the E1 protein enhances E2 transcription function in a manner that suggests the E1 protein itself can contribute to transcriptional regulation not simply by E2 stabilisation but by direct stimulation of transcription. This activation of E2 transcription is again dependent upon an interaction with E1. Overall the results suggest that in the viral life cycle, co-expression of E1 with E2 can increase E2 stability and enhance E2 function.
authors: MRC-University of Glasgow Centre for Virus Research, Institute of Infection Immunity and Inflammation, College of Medical Veterinary and Life Sciences, University of Glasgow, Garscube Estate, Glasgow G61 1QH, UK.
authors: Lauren E
authors: LE
authors: King
authors: Edward S
authors: ES
authors: Dornan
authors: Mary M
authors: MM
authors: Donaldson
authors: Iain M
authors: IM
authors: Morgan
mesh_terms: D002460:Cell Line; D004268:DNA-Binding Proteins / Q000378:metabolism*; D052162:Human papillomavirus 16 / Q000502:physiology*; D006801:Humans; D009856:Oncogene Proteins, Viral / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping; D015533:Transcriptional Activation; D014779:Virus Replication
chemical_list: D004268:DNA-Binding Proteins; C093478:E1 protein, Human papillomavirus 16; C054855:E2 protein, Human papillomavirus type 16; D009856:Oncogene Proteins, Viral