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EMBO J. 2001 May 1;20(9):2315-25.

A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization.

Author information

1
Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.

Abstract

A 340 nucleotide element within the 3' untranslated region of Vg1 mRNA determines its localization to the vegetal cortex of Xenopus oocytes. To identify protein factors that bind to this region, we screened a cDNA expression library with an RNA probe containing this sequence. Five independent isolates encoded a protein (designated Prrp for proline-rich RNA binding protein) having two RNP domains followed by multiple polyproline segments. Prrp and Vg1 mRNAs are co-localized to the vegetal cortex of stage IV oocytes, substantiating an interaction between the two in vivo. Prrp also associates with VegT mRNA, which like Vg1 mRNA uses the late localization pathway, but not with Xcat-2 or Xwnt-11 mRNAs, which use the early pathway. The proline-rich domain of Prrp interacts with profilin, a protein that promotes actin polymerization. Prrp can also associate with the EVH1 domain of Mena, another microfilament-associated protein. Since the anchoring of Vg1 mRNA to the vegetal cortex is actin dependent, one function of Prrp may be to facilitate local actin polymerization, representing a novel function for an RNA binding protein.

PMID:
11331596
PMCID:
PMC125447
DOI:
10.1093/emboj/20.9.2315
[Indexed for MEDLINE]
Free PMC Article

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