University of Sussex
Browse

File(s) not publicly available

Investigation of multimerisation region of the KSHV (HHV8) encoded protein K-bZIP: the proposed leucine zipper region encodes a multimerisation domain with an unusual structure

journal contribution
posted on 2023-06-08, 07:43 authored by Salama Al Mehairi, Eleonora Cerasoli, Alison Sinclair
The K8 gene of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) shares many functional similarities with the BZLF1 gene of Epstein-Barr virus. The protein products of K8 and BZLF1, K-bZIP (RAP, K8) and Zta (BZLF1, ZEBRA, Z) have both been proposed to be members of the bZIP family of transcription factors, forming multimers via a coiled-coil motif termed a leucine zipper. Substantial evidence supporting this model for Zta is published. Here, we demonstrate that the proposed leucine zipper region of K-bZIP (amino acids 182 to 218) is required for multimer formation but that it does not fold as a coiled coil.

History

Publication status

  • Published

Journal

Journal of Virology

ISSN

0022-538X

Publisher

American Society for Microbiology

Issue

12

Volume

79

Page range

7905-7910

Pages

6.0

Department affiliated with

  • Biochemistry Publications

Notes

This research was undertaken in Dr Sinclair's laboratory. This is the first biophysical investigation of the K-bZIP protein encoded by KSHV. The conclusions presented alter the working model of the physical structure of K-bZIP.

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

Usage metrics

    University of Sussex (Publications)

    Categories

    No categories selected

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC