Pirh2 is one of several ubiquitin ligases known to modify and negatively regulate p53. Solution studies reveal the structures of the three Pirh2 domains and indicate that the C-terminal domain of Pirh2 interacts with the p53 tetramerization domain. Additional data suggest that Pirh2 preferentially modifies the tetrameric, transcriptionally active form of p53 for proteasome-mediated degradation.

The ATP-dependent chromatin-remodeling complexes are involved in repositioning, restructuring and evicting nucleosomes. The EM reconstruction of the RSC remodeler in complex with a nucleosome now gives structural insights into nucleosome interaction during remodeling.

The interactome of eukaryotic chaperonin TRiC/CCT is identified through a genome-wide approach, revealing enrichment in large, multidomain proteins, or components of multimeric complexes, rich in hydrophobic sequences and with high β-sheet propensity. Thus, TRiC substrates are slow-folding proteins with complex topology, which are likely to be more prone to aggregation.

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