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