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.
Publication types
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Antibodies, Monoclonal
-
Carrier Proteins / chemistry
-
Carrier Proteins / genetics
-
Carrier Proteins / metabolism*
-
Cell Nucleus / metabolism
-
DNA Damage
-
DNA Repair
-
DNA-Binding Proteins / metabolism
-
HeLa Cells
-
Humans
-
Poly A / metabolism*
-
Proliferating Cell Nuclear Antigen / metabolism
-
RNA Polymerase II / metabolism*
-
RNA Precursors / metabolism*
-
RNA, Messenger / metabolism*
-
RNA-Binding Proteins / chemistry
-
RNA-Binding Proteins / genetics
-
RNA-Binding Proteins / metabolism*
-
Rad51 Recombinase
-
Recombinant Fusion Proteins / metabolism
-
Repetitive Sequences, Amino Acid
-
Tumor Suppressor Proteins*
-
Ubiquitin-Protein Ligases*
-
Zinc Fingers
-
mRNA Cleavage and Polyadenylation Factors
Substances
-
Antibodies, Monoclonal
-
Carrier Proteins
-
DNA-Binding Proteins
-
Proliferating Cell Nuclear Antigen
-
RNA Precursors
-
RNA, Messenger
-
RNA-Binding Proteins
-
Recombinant Fusion Proteins
-
Tumor Suppressor Proteins
-
mRNA Cleavage and Polyadenylation Factors
-
Poly A
-
BARD1 protein, human
-
Ubiquitin-Protein Ligases
-
RAD51 protein, human
-
RNA Polymerase II
-
Rad51 Recombinase