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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00481773" target="_blank" >RIV/61388963:_____/17:00481773 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/17:10369473

Result on the web

<a href="http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0186982" target="_blank" >http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0186982</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1371/journal.pone.0186982" target="_blank" >10.1371/journal.pone.0186982</a>

Result language

angličtina

Original language name

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

Original language description

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 (ARD) of the carboxyl-terminus. ARD consists of four arginine rich subdomains, ARDI, ARDII, ARDIII and ARDIV. Mutation analysis of ARDs revealed that arginine methylation of HBc required the wild-type status of both ARDI and ARDII. Mass spectrometry analysis of HBc identified multiple potential ubiquitination, methylation and phosphorylation sites, out of which lysine K7 and arginines R150 (within ARDI) and R156 (outside ARDs) were shown to be modified by ubiquitination and methylation, respectively. The HBc symmetric dimethylation appeared to be linked to serine phosphorylation and nuclear import of HBc protein. Conversely, the monomethylated HBc retained in the cytoplasm. Thus, overexpression of PRMT5 led to increased nuclear accumulation of HBc, and vice versa, down-regulation of PRMT5 resulted in reduced levels of HBc in nuclei of transfected cells. In summary, we identified PRMT5 as a potent controller of HBc cell trafficking and function and described two novel types of HBc post-translational modifications (PTMs), arginine methylation and ubiquitination.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10607 - Virology

Project

<a href="/en/project/LK11207" target="_blank" >LK11207: The Role of HIV Fitness on Disease Progression in the Absence of Antiretroviral Treatment</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

PLoS ONE

ISSN

1932-6203

e-ISSN

—

Volume of the periodical

12

Issue of the periodical within the volume

10

Country of publishing house

US - UNITED STATES

Number of pages

28

Pages from-to

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UT code for WoS article

000413568900058

EID of the result in the Scopus database

2-s2.0-85032028074