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Association of AUUUA-binding protein with A+U-rich mRNA during nucleo-cytoplasmic transport.

Journal of Molecular Biology

Uridine, Adenosine, Animals, Base Sequence, Binding Sites, Carrier Proteins, metabolism, Cell Line, Cell Nucleus, Cytoplasm, Endoribonucleases, Granulocyte-Macrophage Colony-Stimulating Factor, Humans, Interferon-alpha, genetics, Interleukin-3, Kinetics, Liver, Molecular Sequence Data, Nuclear Envelope, Nuclear Matrix, Plasmids, Polyribonucleotides, Protein Binding, RNA, Messenger, Rats, Ribonucleoproteins, isolation & purification, Transcription, Genetic

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      Resealed nuclear envelope (NE) vesicles from rat liver containing entrapped exogenous RNA were used to study the effect of adenosine+uridine binding factor (AUBF), present in cytosolic cell extracts, on ATP-dependent transport of A+U-rich RNA (AU+RNA) and A+U-free RNA (AU-RNA) across the NE. This factor specifically binds to A+U-rich sequences present in the 3' untranslated regions of lymphokine and cytokine mRNAs, containing overlapping AUUUA boxes (granulocyte-macrophage colony stimulating factor, interleukin-3). Addition of AUBF to the extravesicular compartment markedly increased the efflux of the in vitro transcribed, capped and polyadenylated AU+ RNAs. Export of entrapped AU- control RNA, such as beta-globin RNA, was not affected by AUBF, in contrast to chimeric AU+ beta-globin RNA containing the A+U-rich sequence of human interferon-alpha mRNA (6 reiterated AUUUA motifs). Competition experiments revealed that AUBF enhances the affinity of poly(A)-containing AU+ RNAs to the NE poly(A)-binding component (poly(A)-recognizing mRNA carrier p106), and thereby accelerates nuclear export of these RNAs. We could demonstrate that AUBF added to the extravesicular space forms stable complexes with polyadenylated AU+ RNA with relative molecular masses of about 45,000, 62,000 and 70,000 inside the vesicles or during ATP-dependent export. In addition we determined that AUBF may affect mRNA stability by protecting A+U-rich RNA against degradation by trans-acting, nuclear matrix-associated and A+U-specific endoribonuclease V.

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