Dataset Information

PRMT5: a Novel Regulator of Hepatitis B Virus Replication and an Arginine Methylase of HBV Core

ABSTRACT: In the study, we identified protein arginine methyltransferase 5 (PRMT5) as a novel restriction factor of HBV replication. We have also demonstrated that PRMT5 can interact with the HBV core and methylate its arginine residues within arginine-rich domain. We identified two types of HBc post-translational modifications: arginine methylation and ubiquitination. While monomethylated HBc retains cytoplasmic localization, symmetric dimethylation is linked to serine phosphorylation and nuclear transport. Thus arginine methylation and ubiquitination are novel types of HBc post-translational modifications which add another level of complexity to the understanding of HBc function and regulation of HBV replication

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human) Hepatitis B Virus

TISSUE(S): Hepatocyte, Cell Culture

SUBMITTER: Martin Hubalek

LAB HEAD: Martin Hubalek

PROVIDER: PXD006828 | Pride | 2017-11-01

REPOSITORIES: Pride

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PRMT5: A novel regulator of Hepatitis B virus replication and an arginine methylase of HBV core.

Lubyova Barbora B Hodek Jan J Zabransky Ales A Prouzova Hana H Hubalek Martin M Hirsch Ivan I Weber Jan J

PloS one 20171024 10

In mammals, protein arginine methyltransferase 5, PRMT5, is the main type II enzyme responsible for the majority of symmetric dimethylarginine formation in polypeptides. Recent study reported that PRMT5 restricts Hepatitis B virus (HBV) replication through epigenetic repression of HBV DNA transcription and interference with encapsidation of pregenomic RNA. Here we demonstrate that PRMT5 interacts with the HBV core (HBc) protein and dimethylates arginine residues within the arginine-rich domain ( ...[more]

PMID: 29065155

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			Action	DRS
	BeadsExp1.group	Other
	BeadsExp1.mgf	Mgf
	BeadsExp1.wiff	Wiff
	BeadsExp1.wiff.scan	Wiff
	GelExp_1-14.group	Other