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Chemicals that modulate the acetylation of nuclear proteins have proved instrumental in experimental models of several human diseases.
HDACs can also modulate the acetylation state and activity of major transcription factors [10].
sirtuins) [6], are conserved in all domains of life, and together, GNATs and sirtuins modulate the acetylation state of proteins involved in diverse cellular processes.
While HDAC activity is generally associated with transcriptional repression, through the deacetylation of histones, HDACs may also modulate the acetylation state of major transcription factors, and thus have complex effects on gene regulation.
Despite the knowledge of HDACs and HATs that are reported to modulate the acetylation dynamics of Ku70, very little is known about proteins that critically coordinate these key modifications.
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Through deacetylating acetylated lysine 40 in α-tubulin, Hdac6 modulates the acetylation of microtubules (Hubbert et al., 2002).
Here, we report data in support of the notion that bacteria can control gene expression by modulating the acetylation state of transcription factors (TFs).
The nuclear HS can also regulate gene expression by modulating the acetylation status of histone proteins.
These results demonstrate that HDAC6 directly modulates the acetylation of tau by specifically deacetylating KIGS motifs.
Deprotection of genomic DNA regions can be triggered by modulating the acetylation of histone octamers.
As SMAR1 modulates the acetylation status of Ku70, we investigated for any possible correlation between SMAR1 expression and Ku70 Bax association.
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