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Functional Interaction of BRCA1-Associated BARD1 with Polyadenylation Factor CstF-50
Abstract
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.
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Cited by
Cancer Susceptibility and the Functions of BRCA1 and BRCA2
Venkitaraman, A. R. (2002) · Cell · doi:10.1016/s0092-8674(02)00615-3 · Cited by 1,713
Hashizume, R., Fukuda, M., Maeda, I., Nishikawa, H., Oyake, D., Yabuki, Y., Ogata, H., & Ohta, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c000881200 · Cited by 634
BRCA1–BARD1 promotes RAD51-mediated homologous DNA pairing
Zhao, W., Steinfeld, J. B., Liang, F., Chen, X., Maranon, D. G., Jian Ma, C., Kwon, Y., Rao, T., Wang, W., Sheng, C., et al. (2017) · Nature · doi:10.1038/nature24060 · Cited by 393
Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex
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3′ end mRNA processing: molecular mechanisms and implications for health and disease
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Metadata
- Authors
- Kleiman, F. E., & Manley, J. L.
- Venue
- Science
- Published
- 1999-09-03
- Volume
- 285
- Issue
- 5433
- Pages
- 1576-1579
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2081027578
- Cited by
- 193
- References
- 1
- FWCI
- 5.65
- Type
- journal article
- Language
- en
- Open access
- closed
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