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Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1

journal contribution
posted on 2023-06-07, 21:14 authored by Matthew R. Hicks, Sara Balesaria, Cahora Medina-Palazon, Maya J. Pandya, Derek N. Woolfson, Alison Sinclair
BZLF1 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.

History

Publication status

  • Published

Journal

Journal of Virology

ISSN

0022-538X

Publisher

American Society for Microbiology

Issue

11

Volume

75

Page range

5381-5384

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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