Skip to content

Research at St Andrews

ChlR1 is required for loading papillomavirus E2 onto mitotic chromosomes and viral genome maintenance.

Research output: Contribution to journalArticle

Author(s)

Joanna Louise Parish, AM Bean, RB Park, EJ Androphy

School/Research organisations

Abstract

Autonomously replicating DNA viruses must evade mitotic checkpoints and actively partition their genomes to maintain persistent infection. The E2 protein serves these functions by tethering papillomavirus episomes to mitotic chromosomes; however, the mechanism remains unresolved. We show that E2 binds ChIR1, a DNA helicase that plays a role in sister chromatid cohesion. The E2 mutation W130R falls to bind ChIR1 and correspondingly does not associate with mitotic chromosomes. Viral genomes encoding this E2 mutation are not episomally maintained in cell culture. Notably, E2 W130R binds Brd4, which reportedly acts as a mitotic tether, indicating this interaction is insufficient for E2 association with mitotic chromosomes. RNAi-induced depletion of ChIR1 significantly reduced E2 localization to mitotic chromosomes. These studies provide compelling evidence that ChIR1 association is required for loading the papillomavirus E2 protein onto mitotic chromosomes and represents a kinetochore-independent mechanism for viral genome maintenance and segregation.

Close

Details

Original languageEnglish
Pages (from-to)867-876
Number of pages10
JournalMolecular Cell
Volume24
Issue number6
DOIs
Publication statusPublished - 28 Dec 2006

    Research areas

  • SISTER-CHROMATID COHESION, SARCOMA-ASSOCIATED HERPESVIRUS, TRANSCRIPTIONAL ACTIVATION FUNCTION, BROMODOMAIN PROTEIN BRD4, NUCLEAR ANTIGEN 1, BOVINE PAPILLOMAVIRUS, SACCHAROMYCES-CEREVISIAE, DNA HELICASE, TYPE-1 E2, TRANSACTIVATION DOMAIN

Discover related content
Find related publications, people, projects and more using interactive charts.

View graph of relations

Related by journal

  1. Non-canonical activation of the DNA sensing adaptor STING by ATM and IFI16 mediates NF-κB signalling after nuclear DNA damage

    Dunphy, G., Flannery, S. M., Almine, J. F., Connolly, D. J., Paulus, C., Jonsson, K. L., Jakobsen, M. R., Nevels, M. M., Bowie, A. G. & Unterholzner, L., 6 Sep 2018, In : Molecular Cell. 71, 5, p. 745-760 22 p., e5.

    Research output: Contribution to journalArticle

  2. Structure of the CRISPR Interference complex CSM reveals key similarities with Cascade

    Rouillon, C., Zhou, M., Zhang, J., Argyris, P., Beilsten-Edmands, V., Cannone, G., Graham, S., Robinson, C., Spagnolo, L. & White, M. F., 10 Oct 2013, In : Molecular Cell. 52, 1, p. 124-134 11 p.

    Research output: Contribution to journalArticle

  3. Structure and mechanism of the CMR complex for CRISPR-Mediated antiviral immunity

    Zhang, J., Rouillon, C., Kerou, M., Reeks, J., Brugger, K., Graham, S., Reimann, J., Cannone, G., Liu, H., Albers, S-V., Naismith, J. H., Spagnolo, L. & White, M. F., 10 Feb 2012, In : Molecular Cell. 45, 3, p. 303-313 11 p.

    Research output: Contribution to journalArticle

  4. The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation

    Bowman, A., Ward, R., Wiechens, N., Singh, V., El Mkami, H., Norman, D. G. & Owen-Hughes, T., 18 Feb 2011, In : Molecular Cell. 41, 4, p. 398-408 11 p.

    Research output: Contribution to journalArticle

ID: 382895