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(2003). Poly(A)-binding protein positively affects YB-1 mRNA translation through specific interaction with YB-1 mRNAстатья
- Авторы: Skabkina O.V., Skabkin M.A., Popova N.V., Lyabin D.N., Penalva L.O., Ovchinnikov L.P.
- Журнал: The Journal of biological chemistry
- Том: 278
- Номер: 20
- Год издания: 2003
- Первая страница: 18191
- Последняя страница: 18198
- DOI: 10.1074/jbc.M209073200
- Аннотация: 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.
- Добавил в систему: Лябин Дмитрий Николаевич