Histone Acetyltransferases: Difference between revisions

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An enzyme responsible for the acetylation of lysine residues (by adding an acetyl group) on the N-terminal tails on mRNA during post-translational modification. This is large multi-subunit complex that associates with a number of proteins, including the families GNAT , MYST and p300/CBP (Sterner and Berger, 2000). This in turn is a form of transcriptional regulation as it causes the disruption of chromatin structure.  
An enzyme responsible for the [[acetylation|acetylation]] of [[lysine|lysine]] residues (by adding an [[acetyl group|acetyl group]]) on the [[N-terminal|N-terminal]] tails on [[mRNA|mRNA]] during [[post-translational modification|post-translational modification]]. This is large multi-subunit complex that associates with a number of [[proteins|proteins]], including the families [[GNAT|GNAT]], [[MYST|MYST]] and p300/CBP<ref>Sterner, D. E. and Berger, S. L. (2000) ‘Acetylation of Histones and Transcription-Related Factors’, Microbiology and Molecular Biology Reviews, 64(2), pp. 435–459. doi: 10.1128/mmbr.64.2.435-459.2000</ref>. This in turn is a form of transcriptional regulation as it causes the disruption of [[chromatin|chromatin]] structure.  


=== References ===


 
<references />
Sterner, D. E. and Berger, S. L. (2000) ‘Acetylation of Histones and Transcription-Related Factors’, Microbiology and Molecular Biology Reviews, 64(2), pp. 435–459. doi: 10.1128/mmbr.64.2.435-459.2000

Latest revision as of 12:18, 27 October 2015

An enzyme responsible for the acetylation of lysine residues (by adding an acetyl group) on the N-terminal tails on mRNA during post-translational modification. This is large multi-subunit complex that associates with a number of proteins, including the families GNAT, MYST and p300/CBP[1]. This in turn is a form of transcriptional regulation as it causes the disruption of chromatin structure.

References

  1. Sterner, D. E. and Berger, S. L. (2000) ‘Acetylation of Histones and Transcription-Related Factors’, Microbiology and Molecular Biology Reviews, 64(2), pp. 435–459. doi: 10.1128/mmbr.64.2.435-459.2000