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RNA interaction and cleavage of poly(C)-binding protein 2 by hepatitis A virus protease.

Abstract：

:The poly(rC)-binding protein PCBP2 has multiple functions in post-transcriptional control of host and viral gene expression. Since it interacts with picornaviral RNA structures, it was proposed that PCBP2 regulates viral genome translation and replication. The hepatitis A virus (HAV), an atypical picornavirus, contains an unusual pyrimidine-rich tract (pY1) with unknown functions. Using in vivo and in vitro assays, we provide direct evidence that PCBP2 interacts with pY1 and that binding is mediated by KH domains 1 and 3. Proteolytic cleavage by the viral protease 3C generates a C-terminally truncated polypeptide with highly reduced RNA affinity. The results suggest that during HAV infection PCBP2 cleavage might specifically down-regulate viral protein synthesis, thereby giving way to viral RNA synthesis.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Zhang B,Seitz S,Kusov Y,Zell R,Gauss-Müller V

doi

10.1016/j.bbrc.2007.09.133

subject

Has Abstract

pub_date

2007-12-28 00:00:00

pages

725-30

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)02144-4

journal_volume

364

pub_type

杂志文章

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