Proteasomal turnover of hepatitis C virus core protein is regulated by two distinct mechanisms: a ubiquitin-dependent mechanism and a ubiquitin-independent but PA28gamma-dependent mechanism.

Abstract:

:We have previously reported on the ubiquitylation and degradation of hepatitis C virus core protein. Here we demonstrate that proteasomal degradation of the core protein is mediated by two distinct mechanisms. One leads to polyubiquitylation, in which lysine residues in the N-terminal region are preferential ubiquitylation sites. The other is independent of the presence of ubiquitin. Gain- and loss-of-function analyses using lysineless mutants substantiate the hypothesis that the proteasome activator PA28gamma, a binding partner of the core, is involved in the ubiquitin-independent degradation of the core protein. Our results suggest that turnover of this multifunctional viral protein can be tightly controlled via dual ubiquitin-dependent and -independent proteasomal pathways.

journal_name

J Virol

journal_title

Journal of virology

authors

Suzuki R,Moriishi K,Fukuda K,Shirakura M,Ishii K,Shoji I,Wakita T,Miyamura T,Matsuura Y,Suzuki T

doi

10.1128/JVI.01690-08

subject

Has Abstract

pub_date

2009-03-01 00:00:00

pages

2389-92

issue

5

eissn

0022-538X

issn

1098-5514

pii

JVI.01690-08

journal_volume

83

pub_type

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