Poly(A)-binding Protein Positively Affects YB-1 mRNA Translation through Specific Interaction with YB-1 mRNA
Autor: | Maxim A. Skabkin, Nadezhda V. Popova, Dmitry N. Lyabin, Lev P. Ovchinnikov, Luiz O. F. Penalva, Olga V. Skabkina |
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Rok vydání: | 2003 |
Předmět: |
Sucrose
DNA Complementary Reticulocytes Time Factors Ultraviolet Rays Immunoblotting Biology Inhibitory postsynaptic potential Poly(A)-Binding Proteins Biochemistry P-bodies Gene expression Poly(A)-binding protein Protein biosynthesis Animals RNA Messenger Molecular Biology Messenger RNA Cell-Free System Dose-Response Relationship Drug Temperature Nuclear Proteins Translation (biology) Cell Biology Blotting Northern Precipitin Tests Molecular biology Globins DNA-Binding Proteins NFI Transcription Factors Gene Expression Regulation Cytoplasm Protein Biosynthesis CCAAT-Enhancer-Binding Proteins Codon Terminator biology.protein Electrophoresis Polyacrylamide Gel Rabbits Y-Box-Binding Protein 1 Plasmids Protein Binding Transcription Factors |
Zdroj: | Journal of Biological Chemistry. 278:18191-18198 |
ISSN: | 0021-9258 |
DOI: | 10.1074/jbc.m209073200 |
Popis: | The major protein of cytoplasmic mRNPs from rabbit reticulocytes, YB-1, is a member of an ancient family of proteins containing a common structural feature, cold-shock domain. In eukaryotes, this family is represented by multifunctional mRNA/Y-box DNA-binding proteins that control gene expression at different stages. To address possible post-transcriptional regulation of YB-1 gene expression, we examined effects of exogenous 5'- and 3'-untranslatable region-containing fragments of YB-1 mRNA on its translation and stability in a cell-free system. The addition of the 3' mRNA fragment as well as its subfragment I shut off protein synthesis at the initiation stage without affecting mRNA stability. UV cross-linking revealed four proteins (69, 50, 46, and 44 kDa) that specifically interacted with the 3' mRNA fragment; the inhibitory subfragment I bound two of them, 69- and 50-kDa proteins. We have identified these proteins as PABP (poly(A)-binding protein) (69 kDa) and YB-1 (50 kDa) and demonstrated that titrating out of PABP by poly(A) strongly and specifically inhibits YB-1 mRNA cap(+)poly(A)(-) translation in a cell-free system. Thus, PABP is capable of positively affecting YB-1 mRNA translation in a poly(A) tail-independent manner. |
Databáze: | OpenAIRE |
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