Journal of Biological Chemistry · 1995 · 172 citations · 29 references
Life SciencesGeneticsMolecular BiologyGene ExpressionNucleic Acid BiochemistryProtein TranslationProtein SynthesisRna-binding ProteinsTranslation ControlTranslation In EukaryotesTranslation RegulationTranslational RegulationMessenger Ribonucleic Acid (Mrna) TranslationRna Secondary StructureRna-binding Protein Regulation Of TranslationRna-binding Proteins In TranslationSecondary Rna Structure
A cDNA encoding the major core protein, p50, of cytoplasmic messenger ribonucleoprotein particles (mRNPs) of somatic cells was cloned from a rabbit reticulocyte cDNA library. From the derived 324-amino acid sequence, p50 is identified as a member of the Y-box binding transcription factor family. The protein was earlier described as a repressor of globin mRNA translation. These findings suggest that p50 may affect protein biosynthesis at two levels: mRNA transcription in the nucleus and mRNA translation in the cytoplasm. Together with recently published results showing that masked mRNA in germ cells also is associated with proteins of the Y-box binding protein family, the present finding indicates that these proteins are universal core proteins responsible for the formation of cytoplasmic mRNPs in eukaryotes. Highly purified p50 forms large 18 S homomultimeric complexes with a molecular mass of about 800 kilodaltons and melts RNA secondary structure. This suggests that p50 may affect translation by changing the overall structure of the mRNA.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
Douglas A. Melton, Paul A. Krieg, Michael R. Rebagliati et al. · Nucleic Acids Research · 1984 · 6.4K citations · Full text
3′-Terminal labelling of RNA with T4 RNA ligase
Thomas E. England, Olke C. Uhlenbeck · Nature · 1978 · 561 citations