Structure and function of a human TAFII250 double bromodomain module.

By R. Jacobson, A. Ladurner, D. King, R. Tjian. Science, 2000

902 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/4ac1335eec2e566390575b0a0c4f9236cba87b5d

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

Citations in the corpus

A clustering approach for identification of enriched domains from histone modification ChIP-Seq data (2009, neutral): “In addition to histone methylation, the more dynamic histone acetylation marks also cluster, and several histone acetyltransferases contain bromodomains that specifically bind acetylated histones (Jacobson et al., 2000; Owen et al., 2000; Dodd et al., 2007).”
Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4. (2007, background): “The TAF1 subunit of metazoan TFIID contains an acetyl-lysine binding activity residing in its double bromodomain (Jacobson et al., 2000).”
Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. (2001, background): “Thus far, acetyllysines and methyl-lysine 9 have been found to be recognized by bromodomain- (Dhalluin et al. 1999; Jacobson et al. 2000) and chromodomain-containing polypeptides (Bannister et al.”
The nucleosome: from genomic organization to genomic regulation. (2004, background): “…bent conformation with specific interactions KD of 40 M, whereas it binds a doubly acetylated H4 tail at KD of 1 M, suggesting cooperativity in the dualforming with the side chain of acetyllysine 16 and numerous backbone contacts forming with the adjacent resi- interaction (Jacobson et al., 2000).”
Histone Recognition and Large-Scale Structural Analysis of the Human Bromodomain Family (2012, background): “In contrast, the two BRDs in TAF1 are free to orient independently as shown by the different domain orientations in the dual-domain structure determined here and a previously published model (Jacobson et al., 2000) (Figure 1C).”
Orchestrated response: a symphony of transcription factors for gene control. (2000, background): “X-ray structural analysis combined with quantitative binding assays revealed that the double bromodomain of TAF250 specifically recognized a di-acetylated histone H4 tail peptide but not a control acetylated peptide (Jacobson et al. 2000).”
Histone acetylation: a switch between repressive and permissive chromatin (2002, background): “For example, the bromodomain, found in both Gcn5 and Swi2 (Winston and Allis, 1999), has an affinity for the H4 tail, and this is much enhanced by acetylation at defined lysines (Jacobson et al., 2000; Owen et al., 2000).”