A Xenopus protein related to hnRNP I has a role in cytoplasmic RNA localization

被引：202

作者：

Cote, CA ^{[1
]}

Gautreau, D ^{[1
]}

Denegre, JM ^{[1
]}

Kress, TL ^{[1
]}

Terry, NA ^{[1
]}

Mowry, KL ^{[1
]}

机构：

[1] Brown Univ, Dept Biochem Mol Biol & Cell Biol, Providence, RI 02912 USA

来源：

MOLECULAR CELL | 1999年 / 4卷 / 03期

关键词：

D O I：

10.1016/S1097-2765(00)80345-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cytoplasmic localization of mRNA molecules is a powerful mechanism for generating cell polarity. II? 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.

引用

页码：431 / 437

页数：7

共 45 条

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