BRCA1 is a component of the RNA polymerase II holoenzyme Export

@article{citeulike:2755374, abstract = {The familial breast-ovarian tumor suppressor gene product BRCA1 was found to be a component of the RNA polymerase II holoenzyme by several criteria. BRCA1 was found to copurify with the holoenzyme over multiple chromatographic steps. Other tested transcription activators that could potentially contact the holoenzyme were not stably associated with the holoenzyme as determined by copurification. Antibody specific for the holoenzyme component hSRB7 specifically purifies BRCA1. Immunopurification of BRCA1 complexes also specifically purifies transcriptionally active RNA polymerase II and transcription factors TFIIF, TFIIE, and TFIIH. Moreover, a BRCA1 domain, which is deleted in about 90\% of clinically relevant mutations, participates in binding to the holoenzyme complex in cells. These data are consistent with recent data identifying transcription activation domains in the BRCA1 protein and link the BRCA1 tumor suppressor protein with the transcription process as a holoenzyme-bound protein. 10.1073/pnas.94.11.5605}, author = {Scully, Ralph and Anderson, Stephen F. and Chao, David M. and Wei, Wanjiang and Ye, Liyan and Young, Richard A. and Livingston, David M. and Parvin, Jeffrey D.}, citeulike-article-id = {2755374}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.94.11.5605}, citeulike-linkout-1 = {http://www.pnas.org/cgi/content/abstract/94/11/5605}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/9159119}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=9159119}, day = {27}, doi = {10.1073/pnas.94.11.5605}, journal = {Proceedings of the National Academy of Sciences}, keywords = {brca1, holoenzyme, ii, pol, transcription}, month = {May}, number = {11}, pages = {5605--5610}, posted-at = {2008-05-05 08:21:01}, priority = {5}, title = {BRCA1 is a component of the RNA polymerase II holoenzyme}, url = {http://dx.doi.org/10.1073/pnas.94.11.5605}, volume = {94}, year = {1997} }

TY - JOUR ID - citeulike:2755374 L3 - citeulike-article-id:2755374 N2 - The familial breast-ovarian tumor suppressor gene product BRCA1 was found to be a component of the RNA polymerase II holoenzyme by several criteria. BRCA1 was found to copurify with the holoenzyme over multiple chromatographic steps. Other tested transcription activators that could potentially contact the holoenzyme were not stably associated with the holoenzyme as determined by copurification. Antibody specific for the holoenzyme component hSRB7 specifically purifies BRCA1. Immunopurification of BRCA1 complexes also specifically purifies transcriptionally active RNA polymerase II and transcription factors TFIIF, TFIIE, and TFIIH. Moreover, a BRCA1 domain, which is deleted in about 90% of clinically relevant mutations, participates in binding to the holoenzyme complex in cells. These data are consistent with recent data identifying transcription activation domains in the BRCA1 protein and link the BRCA1 tumor suppressor protein with the transcription process as a holoenzyme-bound protein. 10.1073/pnas.94.11.5605 IS - 11 JF - Proceedings of the National Academy of Sciences EP - 5610 TI - BRCA1 is a component of the RNA polymerase II holoenzyme VL - 94 SP - 5605 KW - brca1 KW - holoenzyme KW - ii KW - pol KW - transcription AU - Scully, Ralph AU - Anderson, Stephen AU - Chao, David AU - Wei, Wanjiang AU - Ye, Liyan AU - Young, Richard AU - Livingston, David AU - Parvin, Jeffrey PY - 1997/05/27/ UR - http://dx.doi.org/10.1073/pnas.94.11.5605 ER -