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
Rok vydání: 2003
Předmět:
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