Press Release


About Histone Acylation, Chromatin Dynamics and Metabolism...

Post-translational histone modifications (PTMs) are an important means to open up the chromatin structure for all nuclear processes that require the DNA as template. The identification of novel types of PTMs in addition to the four most prominent ones has added another level of complexity to the regulation of chromatin dynamics. In a review article published recently in Embo Reports, a group of researchers of the Institute of Functional Epigenetics describe the current technical limitations and provide an overview of approaches, when it comes to studying novel PTMs.

Metabolic Subnuclear Niches; @Embo Reports

The packaging of the DNA within the nucleus influences transcription – the fundamental process that generates transportable messenger RNA molecules, which transport the information how a specific protein needs to look like to the protein production machineries – and post-translational histone modifications (PTMs) influence how the DNA is packaged. Over more than 50 years, research has devoted to shed light into the role of PTMs in different biological processes, including transcription.

Histone lysine acetylation, a PTM that belongs to the chemical group of lysine acylation, is one of the most prominent and best studied histone PTM. Histone acetylation has the capacity to destabilizing the fundamental units of chromatin thereby opening up the chromatin structure and making the DNA accessible for e.g., the transcription machinery. 

The first PTM (phosphorylation) was identified more than 60 years ago. Since then, a remarkable series of findings have proven their importance for regulating transcription and other DNA-templated processes. Yet, there is still a lot to learn about histone PTMs. Moreover, novel types of histone PTMs have recently entered the field, including other types of histone acylation. The laboratory of Prof. Schneider at the Institute of Functional Epigenetics is world-leading in the field of PTM research shedding light on how the novel types of PTMs can contribute mechanistically to the regulation of transcriptional activity.

Just recently, he published together with his PhD student Sandra Nitsch and his former Postdoc Dr. Lara Shahidian a review article in Embo Reports about histone acylation, how it impacts the chromatin structure and transcription, and how metabolic fluctuations within the cell might influence histone acylation levels. They further describe the technical challenges that complicate the study of novel PTMs like acylation, and give an overview of approaches to study histone acylation. 

If you would like to read the full article, please go here