| pmid | 10477523 | ||
|---|---|---|---|
| title | Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50. | ||
| authors |
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| journal | Science | ||
| year | 1999 | ||
| full_text_available | false | ||
| doi | 10.1126/science.285.5433.1576 |
Authors: Kleiman FE, Manley JL Journal: Science (1999) DOI: 10.1126/science.285.5433.1576
- Science. 1999 Sep 3;285(5433):1576-9. doi: 10.1126/science.285.5433.1576.
Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50.
Kleiman FE(1), Manley JL.
Author information: (1)Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
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.
DOI: 10.1126/science.285.5433.1576 PMID: 10477523 [Indexed for MEDLINE]