RNA interaction and cleavage of poly(C)-binding protein 2 by hepatitis A virus protease.
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.
Zhang
Bo
B
Institute of Medical Molecular Biology, University of Lübeck, Germany.
Seitz
Simone
S
Kusov
Yuri
Y
Zell
Roland
R
Gauss-Müller
Verena
V
D001665:Binding Sites; D030041:Hepatitis A virus / Q000737:chemistry* / Q000201:enzymology*; D011485:Protein Binding; D012313:RNA / Q000737:chemistry* / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*
C501903:PCBP2 protein, human; D016601:RNA-Binding Proteins; D012313:RNA