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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

The BRCA1 and BARD1 association with the RNA polymerase II holoenzyme.

We have previously shown that endogenous BRCA1 and overexpressed epitope-tagged BRCA1 are present in the transcription complex called the RNA polymerase II holoenzyme (holo-pol). In this study, we further characterized BRCA1 association with the holo-pol by overexpressing deletion mutants of epitope-tagged BRCA1. We found that BRCA1-associated RING domain protein (BARD1) is a component of the holo-pol complex. Deletion of the BRCA1 NH(2) terminus, which is bound by BARD1 as well as other proteins, eliminates >98% of BRCA1 association with the holo-pol. In contrast with earlier observations, deletion of the COOH terminus of BRCA1 did not affect significantly the association with holo-pol. Immunocytochemistry of expressed full-length and deletion mutants of BRCA1 showed that the NH(2) terminus of BRCA1 is important for nuclear dot formation in S-phase. An intact BRCA1 NH(2) terminus is required for the association with holo-pol and for subnuclear localization in S-phase foci. Taken together, these data support a role for BRCA1 regulation of holo-pol function.[1]


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