| Literature DB >> 10518224 |
C A Cote1, D Gautreau, J M Denegre, T L Kress, N A Terry, K L Mowry.
Abstract
Cytoplasmic localization of mRNA molecules is a powerful mechanism for generating cell polarity. In vertebrates, one paradigm is localization of Vg1 RNA within the Xenopus oocyte, a process directed by recognition of a localization element within the Vg1 3' UTR. We show that specific base changes within the localization element abolish both localization in vivo and binding in vitro by a single protein, VgRBP60. VgRBP60 is homologous to a human hnRNP protein, hnRNP I, and combined immunolocalization and in situ hybridization demonstrate striking colocalization of hnRNP I and Vg1 RNA within the vegetal cytoplasm of the Xenopus oocyte. These results implicate a novel role in cytoplasmic RNA transport for this family of nuclear RNA-binding proteins.Entities:
Mesh：
Substances：
Year: 1999 PMID： 10518224 DOI： 10.1016/s1097-2765(00)80345-7
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970