Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics |
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| Authors: | Andrew J Antczak Toshiaki Tsubota Paul D Kaufman James M Berger |
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| Affiliation: | (1) Biotechnology Department, University of the Western Cape, Modderdam Road, Bellville, 7535, South Africa;(2) Department of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, University of Utrecht, Padualaan 8, 3584, CH, Utrecht, The Netherlands;(3) Department of Molecular and Cell Biology, University of the Witwatersrand, 1 Jan Smuts Avenue, Johannesburg, 2050, South Africa;(4) Varian Deutschland GmbH, Alsfelder Straβe 3, D-64289 Darmstadt, Germany |
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| Abstract: | ![]()
Background RBBP6 is a 250 kDa splicing-associated protein that has been identified as an E3 ligase due to the presence of a RING finger domain. In humans and mice it interacts with both p53 and Rb, and plays a role in the induction of apoptosis and regulation of the cell cycle. RBBP6 has recently been shown to be highly up-regulated in oesophageal cancer, and to be a promising target for immunotherapy against the disease. |
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