Malonylation of histone H2A at lysine 119 inhibits Bub1-dependent H2A phosphorylation and chromosomal localization of shugoshin proteins

Scientific Reports
Tadashi IshiguroShigehiro A Kawashima

Abstract

Post-translational modifications of histones, such as acetylation and phosphorylation, are highly conserved in eukaryotes and their combination enables precise regulation of many cellular functions. Recent studies using mass spectrometry have revealed various non-acetyl acylations in histones, including malonylation and succinylation, which change the positive charge of lysine into a negative one. However, the molecular function of histone malonylation or succinylation is poorly understood. Here, we discovered the functions of malonylation in histone H2A at lysine 119 (H2A-K119) in chromosome segregation during mitosis and meiosis. Analyses of H2A-K119 mutants in Saccharomyces cerevisiae and Schizosaccharomyces pombe showed that anionic mutations, specifically to aspartate (K119D) and glutamate (K119E), showed mis-segregation of the chromosomes and sensitivity to microtubule-destabilizing reagents in mitosis and meiosis. We found that the chromosomal localization of shugoshin proteins, which depends on Bub1-catalyzed phosphorylation of H2A at serine 121 (H2A-S121), was significantly reduced in the H2A-K119D and the H2A-K119E mutants. Biochemical analyses using K119-unmodified or -malonylated H2A-C-tail peptides showed that H2A-...Continue Reading

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Citations

Jan 21, 2020·Essays in Biochemistry·Lauren Elizabeth Smith, Adelina Rogowska-Wrzesinska
May 24, 2020·Nature Chemical Biology·Katharine L Diehl, Tom W Muir
Nov 3, 2020·Current Opinion in Biotechnology·Dylan G RyanLuke Aj O'Neill
Jun 23, 2021·Current Opinion in Chemical Biology·Sarah FaulknerYael David

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Methods Mentioned

BETA
histone acetylation
acetylation
acylation
immunoprecipitation
amino
acid
pulled down
pull-down
PCR
ChIP

Software Mentioned

PeakView

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