The Human Adenovirus Type 5 E4orf6/E1B55K E3 Ubiquitin Ligase Complex Enhances E1A Functional Activity

Author:

Dallaire Frédéric1,Schreiner Sabrina2,Blair G. Eric3,Dobner Thomas4,Branton Philip E.156,Blanchette Paola1

Affiliation:

1. Department of Biochemistry, McGill University, Montreal, Québec, Canada

2. Institute of Virology, Technische Universität München/Helmholtz Zentrum München, Munich, Germany

3. School of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom

4. Heinrich Pette Institute, Leibniz Institute for Experimental Virology, Hamburg, Germany

5. Department of Oncology, McGill University, Montreal, Québec, Canada

6. The Goodman Cancer Research Centre, McGill University, Montreal, Québec, Canada

Abstract

Following our demonstration that adenovirus E3 ubiquitin ligase formed by the viral E4orf6 and E1B55K proteins is able to mimic the activation of E2F by E1A, we conducted a series of studies to determine if this complex might also promote the ability of E1A to do so. We found that the complex both significantly stabilizes E1A proteins and also enhances their ability to activate E2F. This finding is of significance because it represents an entirely new function for the ligase in regulating adenovirus replication by enhancing the action of E1A products.

Funder

Gouvernement du Canada | CIHR | Institute of Infection and Immunity

Else Kröner-Fresenius-Stiftung

Dräger-Stiftung

Deutsche Krebshilfe e.V.

Deutsche Forschungsgemeinschaft

Wilhelm Sander-Stiftung

Freie und Hansestadt Hamburg

Bundesministerium fur Gesundheit

Yorkshire Cancer Research

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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