Abstract:
BACKGROUND:Protein arginine methyltransferase 6 (PRMT6) is a nuclear enzyme that methylates arginine residues on histones and transcription factors. In addition, PRMT6 inhibits HIV-1 replication in cell culture by directly methylating and interfering with the functions of several HIV-1 proteins, i.e. Tat, Rev and nucleocapsid (NC). PRMT6 also displays automethylation capacity but the role of this post-translational modification in its antiretroviral activity remains unknown. RESULTS:Here we report the identification by liquid chromatography-mass spectrometry of R35 within PRMT6 as the target residue for automethylation and have confirmed this by site-directed mutagenesis and in vitro and in vivo methylation assays. We further show that automethylation at position 35 greatly affects PRMT6 stability and is indispensable for its antiretroviral activity, as demonstrated in HIV-1 single-cycle TZM-bl infectivity assays. CONCLUSION:These results show that PRMT6 automethylation plays a role in the stability of this protein and that this event is indispensible for its anti-HIV-1 activity.
journal_name
Retrovirologyjournal_title
Retrovirologyauthors
Singhroy DN,Mesplède T,Sabbah A,Quashie PK,Falgueyret JP,Wainberg MAdoi
10.1186/1742-4690-10-73subject
Has Abstractpub_date
2013-07-17 00:00:00pages
73issn
1742-4690pii
1742-4690-10-73journal_volume
10pub_type
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