The Major Messenger Ribonucleoprotein Particle Protein p50 (YB-1) Promotes Nucleic Acid Strand Annealing
| Autor: | Maxim A. Skabkin, Lev P. Ovchinnikov, Adri A. M. Thomas, Valentina Evdokimova |
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| Rok vydání: | 2001 |
| Předmět: |
Protein Denaturation
DNA Complementary RNA-binding protein Protein Serine-Threonine Kinases Biology Biochemistry Protein Structure Secondary Nucleic acid thermodynamics chemistry.chemical_compound Nucleic Acids Translational regulation Animals Phosphorylation Nucleic acid structure Casein Kinase II Molecular Biology RNA Double-Stranded Dose-Response Relationship Drug Models Genetic Temperature RNA-Binding Proteins RNA Nucleic Acid Strand DNA Cell Biology Recombinant Proteins Repressor Proteins chemistry Biophysics Nucleic acid Salts Rabbits |
| Zdroj: | Journal of Biological Chemistry. 276:44841-44847 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m107581200 |
| Popis: | p50, a member of the Y-box binding transcription factor family, is tightly associated with eukaryotic mRNAs and is responsible for general translational regulation. Here we show that p50, in addition to its previously described ability to melt mRNA secondary structure, is capable of promoting rapid annealing of complementary nucleic acid strands. p50 accelerates annealing of RNA and DNA duplexes up to 1500-fold within a wide range of salt concentrations and temperatures. Phosphorylation of p50 selectively inhibits DNA annealing. Moreover, p50 catalyzes strand exchange between double-stranded and single-stranded RNAs yielding a product bearing a more extended double-stranded structure. Strikingly, p50 displays both RNA-melting and -annealing activities in a dose-dependent manner; a relatively low amount of p50 promotes formation of RNA duplexes, whereas an excess of p50 causes unwinding of double-stranded forms. Our results suggest that the alteration of nucleic acid conformation is a basic mechanism of the p50-dependent regulation of gene expression. |
| Databáze: | OpenAIRE |
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