Tuning BRCA1 and BARD1 activity to investigate RING ubiquitin ligase mechanisms

The tumor‐suppressor protein BRCA1 works with BARD1 to catalyze the transfer of ubiquitin onto protein substrates. The N‐terminal regions of BRCA1 and BARD1 that contain their RING domains are responsible for dimerization and ubiquitin ligase activity. This activity is a common feature among hundred...

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Veröffentlicht in:	Protein science 2017-03, Vol.26 (3), p.475-483
Hauptverfasser:	Stewart, Mikaela D., Duncan, Emily D., Coronado, Ernesto, DaRosa, Paul A., Pruneda, Jonathan N., Brzovic, Peter S., Klevit, Rachel E.
Format:	Artikel
Sprache:	eng
Schlagworte:	BARD1 BRCA1 BRCA1 protein BRCA1 Protein - chemistry BRCA1 Protein - genetics BRCA1 Protein - metabolism Breast cancer Cancer Dimerization Enzymes Humans Hyperactivity Protein Domains Protein Multimerization Proteins Residues RING domain Substrates Tumor Suppressor Proteins - chemistry Tumor Suppressor Proteins - genetics Tumor Suppressor Proteins - metabolism Tuning Ubiquitin Ubiquitin - chemistry Ubiquitin - genetics Ubiquitin - metabolism ubiquitin E3 ligase Ubiquitin-protein ligase Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitination
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