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The Protein Arginine Methyltransferase PRMT6 Inhibits HIV-1 Tat Nucleolar Retention

The Protein Arginine Methyltransferase PRMT6 Inhibits HIV-1 Tat Nucleolar Retention

Alex J Fulcher, Haran Sivakumaran, Hongping Jin, Daniel J Rawle, David Harrich, David A Jans

Biochim Biophys Acta. 2016 Feb;1863(2):254-62.

PMID: 26611710

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42416114	PRMT6 active human			Price

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