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Science 3 September 1999:
Vol. 285. no. 5433, pp. 1576 - 1579
DOI: 10.1126/science.285.5433.1576

Reports

Functional Interaction of BRCA1-Associated BARD1 with Polyadenylation Factor CstF-50

Frida E. Kleiman, and James L. Manley *

Polyadenylation of messenger RNA precursors requires a complex protein machinery that is closely integrated with the even more complex transcriptional apparatus. Here a polyadenylation factor, CstF-50 (cleavage stimulation factor), is shown to interact in vitro and in intact cells with a nuclear protein of previously unknown function, BRCA1-associated RING domain protein (BARD1). The BARD1-CstF-50 interaction inhibits polyadenylation in vitro. BARD1, like CstF-50, also interacts with RNA polymerase II. These results indicate that BARD1-mediated inhibition of polyadenylation may prevent inappropriate RNA processing during transcription, perhaps at sites of DNA repair, and they reveal an unanticipated integration of diverse nuclear events.

Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
*   To whom correspondence should be addressed. E-mail: jlm2{at}columbia.edu


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Science. ISSN 0036-8075 (print), 1095-9203 (online)