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DOI: http://dx.doi.org/10.7554/eLife.06394.014 The individual cases described in Figure 2 suggest that Hairy organizes a coordinated set of chromatin changes involving both deacetylation and demethylation of multiple histone residues.
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In summary, these results suggest that dSfmbt binds H4K20me1 with high affinity through the combined interaction of the MBT-binding pocket with the mono-methylated lysine and multiple contacts on the MBT surface with histone residues flanking the methyl-lysine.
The multiple types of modifications that take place on specific histone residues and the regulatory cascades that can be triggered in this manner led investigators to propose that a "histone code" regulates gene expression in a manner reminiscent of the genetic code translating nucleic acid coding sequences into protein sequences [ 1, 2].
Dear Editor, A growing body of evidence indicates that several modifications on adjacent nucleosomal histone residues (marks) work in a combinatorial fashion to control access to DNA of multiple proteins involved in transcription, replication and repair.
BRM binds to acetylated histone residues and opens chromatin.
Although it remains to be determined whether BRM directly binds to nucleosomes containing acetylated histone residues, our analysis of the genome-wide distributions of BRM and histone modifications indicated the enrichment of BRM around sites of histone H3K9ac and H3K14ac, suggesting the preferential binding of BRM to these acetylated histone residues in Arabidopsis (Fig. 10b).
Cells regulate transcription by coordinating the activities of multiple histone modifying complexes.
Subsequently, remodeling of the nucleosome allows enzymatic reactions by histone-modifying factors that may acetylate, methylate or demethylate specific histone residues.
Zhou et al. Genome-wide profiling of histone H3 lysine 9 acetylation and dimethylation in Arabidopsis reveals correlation between multiple histone marks and gene expression.
Histone acetylation/deacetylation is often associated with histone methylation changes at specific histone residues.
Methylation and acetylation of individual histone residues are mutually exclusive.
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