Poly(A)-binding protein positively affects YB-1 mRNA translation through specific interaction with YB-1 mRNA.


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.


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@article{Skabkina2003PolyAbindingPP, title={Poly(A)-binding protein positively affects YB-1 mRNA translation through specific interaction with YB-1 mRNA.}, author={Olga V. Skabkina and Maxim A. Skabkin and Nadezhda V Popova and Dmitry N. Lyabin and Luiz O. F. Penalva and Lev P. Ovchinnikov}, journal={The Journal of biological chemistry}, year={2003}, volume={278 20}, pages={18191-8} }