Genetic analysis of the E2 transactivation domain dimerization interface from bovine papillomavirus type 1

Abstract The bovine papillomavirus type 1 (BPV1) E2 protein binds as a dimer to the viral genome to promote its transcription, replication and maintenance in keratinocytes. Although BPV1 E2 dimerizes primarily through its DNA-binding domain, it was shown previously that its transactivation domain (T...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2013-05, Vol.439 (2), p.132-139
Main Authors: Gagnon, David, Sénéchal, Hélène, D’Abramo, Claudia M, Alvarez, Jennifer, McBride, Alison A, Archambault, Jacques
Format: Article
Language:English
Subjects:
Amino Acid Substitution
Bovine papillomavirus 1 - genetics
Bovine papillomavirus 1 - physiology
BPV1
Dimer
Dimerization
DNA Mutational Analysis
DNA replication
DNA, Viral - metabolism
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
High-throughput assay
Humans
Infectious Disease
Mutant Proteins - genetics
Mutant Proteins - metabolism
Protein interface
Protein Multimerization
Redox
Transactivation
Transactivation domain
Viral Proteins - genetics
Viral Proteins - metabolism
Virus Replication
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Summary:Abstract The bovine papillomavirus type 1 (BPV1) E2 protein binds as a dimer to the viral genome to promote its transcription, replication and maintenance in keratinocytes. Although BPV1 E2 dimerizes primarily through its DNA-binding domain, it was shown previously that its transactivation domain (TAD) can also dimerize in vitro through formation of a disulfide bond between cysteine 57 (C57) of adjacent monomers and of an ion pair between arginine 172 (R172) and aspartic acid 175 (D175). The function of this TAD dimerization interface in vivo remains unknown. Here, we report the effects of substituting C57, R172 and D175 by alanine on the transactivation activity of BPV E2 as well as on its ability to support viral DNA replication using a novel luciferase-based assay. Results for this mutational analysis suggest that the TAD dimerization interface is not essential for either process but may contribute to the DNA replication activity of BPV1 E2.
ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2013.02.012