unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA
Article Abstract:
Internal initiation of translation of human rhinovirus (HRV) RNA must have unr, a cellular cytoplasmic RNA-binding protein that has five cold-shock domains. The purification of one of the activities of HeLa cells has been accomplished by using an RNA-affinity column based on the HRV 5' UTR. Two parts were found, one a 38-kD protein, a novel member of the GH-WD repeat protein family having no intrinsic RNA-binding activity and the other a 96-97 kD protein doublet identified as unr. Coimmunoprecipitation with antibodies against either protein shows that they interact with each other.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1999
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A prokaryotic-like mode of cytoplasmic eukaryotic ribosome binding to the initiation codon during internal translation initiation of hepatitis C and classical swine fever virus RNAs
Article Abstract:
Translation of classical swine fever virus and hepatitis C virus mRNAs is initiated by internal ribosomal entry. Reconstitution of internal ribosomal entry in vitro from purified translation components and monitored assembly of 48S ribosomal preinitiation complexes by toe-printing have been carried out. There is cytoplasmic eukaryotic ribosome binding to an initiation codon in internal translation initiation of hepatitis C and classical swine fever virus RNAs. This eukaryotic initiation system is very like translation initiation in prokaryotes.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1998
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Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of elF2-bound GTP
Article Abstract:
Eukaryotic initiation factor (eIF)5 induced hydrolysis of eIF2-bound GTP in 48S complexes led to release of eIF2-GDP. It was observed that the establishment of codon-anticodon base-pairing in 48S complexes relieved eIF's inhibition.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2004
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