Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50.
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.
Mesh Terms:
Antibodies, Monoclonal, Carrier Proteins, Cell Nucleus, DNA Damage, DNA Repair, DNA-Binding Proteins, Hela Cells, Humans, Poly A, Proliferating Cell Nuclear Antigen, RNA Polymerase II, RNA Precursors, RNA, Messenger, RNA-Binding Proteins, Rad51 Recombinase, Recombinant Fusion Proteins, Repetitive Sequences, Amino Acid, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, Zinc Fingers, mRNA Cleavage and Polyadenylation Factors
Antibodies, Monoclonal, Carrier Proteins, Cell Nucleus, DNA Damage, DNA Repair, DNA-Binding Proteins, Hela Cells, Humans, Poly A, Proliferating Cell Nuclear Antigen, RNA Polymerase II, RNA Precursors, RNA, Messenger, RNA-Binding Proteins, Rad51 Recombinase, Recombinant Fusion Proteins, Repetitive Sequences, Amino Acid, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, Zinc Fingers, mRNA Cleavage and Polyadenylation Factors
Science
Date: Sep. 03, 1999
PubMed ID: 10477523
View in: Pubmed Google Scholar
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