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Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1
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posted on 2023-06-07, 21:14 authored by Matthew R. Hicks, Sara Balesaria, Cahora Medina-Palazon, Maya J. Pandya, Derek N. Woolfson, Alison SinclairBZLF1 plays a key role in the induction of Epstein-Barr virus (EBV) replication. On the basis of limited sequence homology and mutagenesis experiments, BZLF1 has been described as a member of the bZip family of transcription factors, but this prospect has not been rigorously tested to date. Here, we present biophysical analysis of the multimerization domain of BZLF1, from three natural variants of EBV, and demonstrate for the first time that the region between amino acids 196 and 227 is sufficient to direct folding as a coiled-coil dimer in vitro.
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Publication status
- Published
Journal
Journal of VirologyISSN
0022-538XPublisher
American Society for MicrobiologyPublisher URL
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11Volume
75Page range
5381-5384Department affiliated with
- Biochemistry Publications
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- No
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- Yes
Legacy Posted Date
2012-02-06Usage metrics
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