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XB-ART-6228
Development 2002 Dec 01;12924:5609-19. doi: 10.1242/dev.00160.
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A homolog of FBP2/KSRP binds to localized mRNAs in Xenopus oocytes.

Kroll TT , Zhao WM , Jiang C , Huber PW .


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A Xenopus oocyte expression library was screened for proteins that bind to the 340-nucleotide localization element of Vg1 mRNA. Four different isolates encoded a Xenopus homolog of the human transcription factor, FUSE-binding protein 2 (FBP2). This protein has been independently identified as the splicing regulatory factor KSRP. The only significant difference between the Xenopus protein, designated VgRBP71, and KSRP is the absence of a 58 amino acid segment near the N-terminal of the former. In vivo binding assays show that VgRBP71 is associated with mRNAs localized to either the vegetal or animal hemispheres, but was not found with control mRNAs. Unlike other factors that bind to the localization element of Vg1 mRNA, VgRBP71 does not accumulate at the vegetal cortex with the mRNA; rather, it is present in the nucleus and throughout the cytoplasm at all stages of oogenesis. Cytoplasmic VgRBP71 appears to be most concentrated at the cell cortex. VgRBP71 interacts with Prrp, another protein that binds to the Vg1 localization element; this association does not require the presence of Vg1 mRNA.

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Species referenced: Xenopus
Genes referenced: actb ddx3x fbp2 fubp1 gdf1 gtf3a khsrp nanos1 prlh vegt wnt11 zfand4
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