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.

United Kingdom, Development and progression, Genetic aspects, Observations, Cellular signal transduction, RNA, Molecular structure, HeLa cells, Poliovirus, Polioviruses, Cytoplasm, Rhinoviruses

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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.

Analysis, Messenger RNA, Codon, Codons, Hepatitis C virus

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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.

Science & research, Genetic research, Hydrolysis

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