The analysis of post-translational modifications of mouse H1 variants by MALDI mass spectrometry

Abstract

The post-translational modifications of linker histone H1 variants from mouse thymus have been studied by MALDI mass spectrometry (matrix-assisted laser desorption/ionization). We have identified six subtypes of histone H1, extracted from the mouse thymus, such as H1.0, H1.1, H1.2, H1.3, H1.4 and H1.5. We have shown that the H1.1 variant is dominant. Analysis of the MS results led us to the conclusion that the types and positions of the posttranslational modifications in H1.2–H1.4 variants within the globular domain are highly conserved. The majority of the identified methylation and acetylation sites of the linker histone H1 subtypes occur in the globular domains of the proteins, e. g. K34, K52, K64, K85 and K97. We have revealed for the first time methylation site of lysine at position 34 in H1.4 (meK34–mH1.4) and H1.1 (meK34–mH1.4) variants. Refs 39. Figs 1. Tables 2.