Project description:In all eukaryotes, acetylation of histones lysine residues correlates with transcription activation. Whether histone acetylation is a cause or consequence of transcription is debated. One model suggests that transcription promotes the recruitment and/or activation of acetyltransferases and histone acetylation occurs as a consequence of ongoing transcription. However, the extent to which transcription shapes the global acetylation landscapes is not known. Here we show that global protein acetylation remains virtually unaltered after acute transcription inhibition. Transcription inhibition ablates the co-transcriptionally occurring ubiquitylation of H2BK120 but does not reduce histone acetylation. The combined inhibition of transcription and CBP/p300 further demonstrates that acetyltransferases remain active and continue to acetylate histones independently of transcription. Together, these results show that histone acetylation is not a mere consequence of transcription; acetyltransferase recruitment and activation is uncoupled from the act of transcription and histone and non-histone protein acetylation are sustained in the absence of ongoing transcription.
Project description:In all eukaryotes, acetylation of histones lysine residues correlates with transcription activation. Whether histone acetylation is a cause or consequence of transcription is debated. One model suggests that transcription promotes the recruitment and/or activation of acetyltransferases and histone acetylation occurs as a consequence of ongoing transcription. However, the extent to which transcription shapes the global acetylation landscapes is not known. Here we show that global protein acetylation remains virtually unaltered after acute transcription inhibition. Transcription inhibition ablates the co-transcriptionally occurring ubiquitylation of H2BK120 but does not reduce histone acetylation. The combined inhibition of transcription and CBP/p300 further demonstrates that acetyltransferases remain active and continue to acetylate histones independently of transcription. Together, these results show that histone acetylation is not a mere consequence of transcription; acetyltransferase recruitment and activation is uncoupled from the act of transcription and histone and non-histone protein acetylation are sustained in the absence of ongoing transcription.
Project description:The acetylation of multiple histone lysine residues in all eukaryotes is known to be associated with transcription activation. However, the causal relationship between histone acetylation and transcription remains a topic of debate. One hypothesis proposes that transcription plays a role in recruiting and activating acetyltransferases, resulting in histone acetylation as a consequence of ongoing transcription. Nevertheless, the extent to which transcription influences the overall acetylation patterns across the genome remains uncertain. This study aims to shed light on this matter by investigating the impact of acute transcription inhibition on global protein acetylation. Surprisingly, the findings demonstrate that global protein acetylation levels remain largely unaffected even after inhibiting transcription. While transcription inhibition leads to the cessation of co-transcriptional ubiquitylation of H2BK120, histone acetylation persists. This suggests that histone acetylation is not solely dependent on transcriptional activity. Moreover, the study delves deeper into the relationship between transcription and acetyltransferase activity. By jointly inhibiting transcription and CBP/p300 it was observed that acetyltransferases remained active and continued to acetylate histones independently of inhibited transcription. Collectively, these results challenge the idea that histone acetylation is merely a consequence of transcription. Instead, they indicate that acetyltransferase recruitment and activation are not directly coupled to the process of transcription. Furthermore, the acetylation of both histone and non-histone proteins persists even in the absence of ongoing transcription. This highlights the complexity of histone acetylation regulation and suggests that it may not be solely dictated by the presence or absence of transcriptional activity.
Project description:mRNA profiles of leukemic B cells from 8-week-old leukemic (Eu-TCL1 and Eu-TCL1-Rab27DKO) mice were generated by 3'-sequencing, in triplicate.
Project description:This SuperSeries is composed of the following subset Series: GSE37697: Antisense Transcripts in Mutant Strains GSE40451: Hrp3 controls nucleosome positioning to suppress non-coding transcription in eu- and heterochromatin [MNase-Seq] Refer to individual Series