The protein arginine methyltransferase PRMT6 inhibits HIV-1 Tat nucleolar retention

Fulcher, Alex J., Sivakumaran, Haran, Jin, Hongpin, Rawle, Daniel J., Harrich, David and Jans, David A. (2016) The protein arginine methyltransferase PRMT6 inhibits HIV-1 Tat nucleolar retention. Biochimica et Biophysica Acta - Molecular Cell Research, 1863 2: 254-262. doi:10.1016/j.bbamcr.2015.11.019

Author Fulcher, Alex J.
Sivakumaran, Haran
Jin, Hongpin
Rawle, Daniel J.
Harrich, David
Jans, David A.
Title The protein arginine methyltransferase PRMT6 inhibits HIV-1 Tat nucleolar retention
Journal name Biochimica et Biophysica Acta - Molecular Cell Research   Check publisher's open access policy
ISSN 0167-4889
Publication date 2016-02
Sub-type Article (original research)
DOI 10.1016/j.bbamcr.2015.11.019
Open Access Status Not Open Access
Volume 1863
Issue 2
Start page 254
End page 262
Total pages 9
Place of publication Amsterdam, NX, Netherlands
Publisher Elsevier
Collection year 2017
Language eng
Abstract The human immunodeficiency virus (HIV)-1 transactivator protein Tat is known to play a key role in HIV infection, integrally related to its role in the host cell nucleus/nucleolus. Here we show for the first time that Tat localisation can be modulated by specific methylation, whereby overexpression of active but not catalytically inactive PRMT6 methyltransferase specifically leads to exclusion of Tat from the nucleolus. An R52/53A mutated Tat derivative does not show this redistribution, implying that R52/53, within Tat's nuclear/nucleolar localisation signal, are the targets of PRMT6 activity. Analysis using fluorescence recovery after photobleaching indicate that Tat nucleolar accumulation is largely through binding to nucleolar components, with methylation of Tat by PRMT6 preventing this. To our knowledge, this is the first report of specific protein methylation inhibiting nucleolar retention.
Keyword HIV-1 Rev
HIV-1 Tat
HTLV-1 Rex
Methyltransferase PRMT6
Nucleolar trafficking
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Public Health Publications
School of Chemistry and Molecular Biosciences
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