Interactome of Site-Specifically Acetylated Linker Histone H1.
Eva HöllmüllerKatharina GreinerSimon M KienleMartin ScheffnerAndreas MarxFlorian StengelPublished in: Journal of proteome research (2021)
Linker histone H1 plays a key role in chromatin organization and maintenance, yet our knowledge of the regulation of H1 functions by post-translational modifications is rather limited. In this study, we report on the generation of site-specifically mono- and di-acetylated linker histone H1.2 by genetic code expansion. We used these modified histones to identify and characterize the acetylation-dependent cellular interactome of H1.2 by affinity purification mass spectrometry and show that site-specific acetylation results in overlapping but distinct groups of interacting partners. Among these, we find multiple translational initiation factors and transcriptional regulators such as the NAD+-dependent deacetylase SIRT1, which we demonstrate to act on acetylated H1.2. Taken together, our data suggest that site-specific acetylation of H1.2 plays a role in modulating protein-protein interactions.
Keyphrases
- transcription factor
- mass spectrometry
- histone deacetylase
- gene expression
- genome wide
- dna damage
- healthcare
- capillary electrophoresis
- electronic health record
- liquid chromatography
- oxidative stress
- signaling pathway
- big data
- ischemia reperfusion injury
- biofilm formation
- dna methylation
- cystic fibrosis
- copy number
- staphylococcus aureus
- high performance liquid chromatography
- machine learning