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Murine gammaherpesvirus 68 ORF75c contains ubiquitin E3 ligase activity and requires PML SUMOylation but not other known cellular PML regulators, CK2 and E6AP, to mediate PML degradation

Issued Date

2013-06-05

Resource Type

Article

ISSN

10960341
00426822

DOI

10.1016/j.virol.2013.02.014

Other identifier(s)

2-s2.0-84876798265

Rights

Mahidol University

Rights Holder(s)

SCOPUS

Bibliographic Citation

Virology. Vol.440, No.2 (2013), 140-149

Suggested Citation

Jaturong Sewatanon, Paul D. Ling Murine gammaherpesvirus 68 ORF75c contains ubiquitin E3 ligase activity and requires PML SUMOylation but not other known cellular PML regulators, CK2 and E6AP, to mediate PML degradation. Virology. Vol.440, No.2 (2013), 140-149. doi:10.1016/j.virol.2013.02.014 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/31907

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Title

Murine gammaherpesvirus 68 ORF75c contains ubiquitin E3 ligase activity and requires PML SUMOylation but not other known cellular PML regulators, CK2 and E6AP, to mediate PML degradation

Author(s)

Jaturong Sewatanon
 Paul D. Ling

Other Contributor(s)

Baylor College of Medicine
 Mahidol University

Abstract

All gammaherpsviruses encode at least one gene related to the cellular formylglycinamide ribonucleotide amidotransferase (FGARAT) enzyme but their biological roles are relatively unknown. The murine gammaherpesvirus 68 (MHV68) vFGARAT, ORF75c, mediates a proteasome-dependent degradation of the antiviral promyelocytic leukemia (PML) protein by an unknown mechanism, which is addressed in this study. We found that ORF75c interacts weakly with PML and SUMO-modified forms of PML are important for its degradation by ORF75c. ORF75c-mediated PML degradation was not dependent on two known cellular regulators of PML stability, Casein kinase II (CK2) and human papilloma virus E6-associated protein (E6AP). Finally, ORF75c had self-ubiquitination activity in vitro and its expression increased levels of ubiquitinated PML in transfected cells. Taken together, the evidence accumulated in this study provides new insights into the function of a vFGARAT and is consistent with a model in which ORF75c could mediate direct ubiquitination of PML resulting in its degradation by the proteasome. © 2013 Elsevier Inc.

Keyword(s)

Immunology and Microbiology

Availability

URI

https://repository.li.mahidol.ac.th/handle/20.500.14594/31907

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