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Vol. 12, Issue 12, 3808-3820, December 2001
Department of Cell and Molecular Biology, Northwestern University
Medical School, Chicago, Illinois 60611
Polypyrimidine tract binding protein, PTB/hnRNP I, is involved in
pre-mRNA processing in the nucleus and RNA localization and translation
in the cytoplasm. In this report, we demonstrate that PTB shuttles
between the nucleus and cytoplasm in an energy-dependent manner.
Deletion mutagenesis demonstrated that a minimum of the N terminus and
RNA recognition motifs (RRMs) 1 and 2 are necessary for
nucleocytoplasmic shuttling. Deletion of RRM3 and 4, domains that are
primarily responsible for RNA binding, accelerated the nucleocytoplasmic shuttling of PTB. Inhibition of transcription directed by either RNA polymerase II alone or all RNA polymerases yielded similar results. In contrast, selective inhibition of RNA
polymerase I did not influence the shuttling kinetics of PTB. Furthermore, the intranuclear mobility of GFP-PTB, as measured by
fluorescence recovery after photobleaching analyses, increased significantly in transcriptionally inactive cells compared with transcriptionally active cells. These observations demonstrate that
nuclear RNA transcription and export are not necessary for the
shuttling of PTB. In addition, binding to nascent RNAs transcribed by
RNA polymerase II and/or III retards both the nuclear export and
nucleoplasmic movement of PTB. The uncoupling of PTB shuttling and RNA
export suggests that the nucleocytoplasmic shuttling of PTB may also
play a regulatory role for its functions in the nucleus and cytoplasm.
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