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© The Rockefeller University Press, 0021-9525/1999//247 $5.00
The Journal of Cell Biology, Volume 147, Number 2, , 1999 247-256

Original Article

The Cis-Acting RNA Trafficking Signal from Myelin Basic Protein mRNA and Its Cognate Trans-Acting Ligand Hnrnp A2 Enhance CaP-Dependent Translation



Sunjong Kwona, Elisa Barbareseb, and John H. Carsona

a Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06030
b Department of Neurology, University of Connecticut Health Center, Farmington, Connecticut 06030
Department of Biochemistry, University of Connecticut Health Center, Farmington, CT 06030.(860) 679-3408(860) 679-2130

jcarson{at}nso2.uchc.edu

The 21 nucleotide RNA trafficking signal (RTS), originally identified in myelin basic protein mRNA, but also found in a variety of other localized RNAs, is necessary and sufficient for transport of RNA along microtubules in oligodendrocytes. The RTS binds specifically to the RNA binding protein, hnRNP A2. Together, the RTS and hnRNP A2 comprise cis/trans determinants for several steps in the RNA trafficking pathway. Here we show that insertion of the RTS into green fluorescent protein (GFP) RNA enhances translation without affecting stability of microinjected RNA. In dicistronic RNA, the RTS enhances cap-dependent translation without affecting internal ribosome entry site (IRES)-dependent translation. The translation enhancer function of the RTS is position, copy number, and cell type independent, hnRNP A2 dependent, and saturable with increasing amounts of injected RNA. This represents one of the first specific translation enhancer elements identified in a mammalian system.

Key Words: translation enhancer • hnRNP A2 • RNA trafficking signal • dicistronic RNA • eIF4E

© 1999 The Rockefeller University Press

1.used in this paper: BFP, blue fluorescent protein; GFP, green fluorescent protein; hnRNP, heterogeneous nuclear RNA binding protein; IF, immunofluorescence; IRES, internal ribosome entry site; MBP, myelin basic protein; RTS, RNA trafficking signal; TRD, Texas red–conjugated dextran

S. Kwon's current address is Department of Cell Biology, Harvard Medical School, Boston, MA 02115.


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J. Cell Biol. 1999 147: 1-2. [Full Text] [PDF]





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