Utilizing targeted mass spectrometry to demonstrate Asf1-dependent increases in residue specificity for Rtt109-Vps75 mediated histone acetylation

PloS One
Yin-Ming KuoAndrew J Andrews

Abstract

In Saccharomyces cerevisiae, Rtt109, a lysine acetyltransferase (KAT), associates with a histone chaperone, either Vps75 or Asf1. It has been proposed that these chaperones alter the selectivity of Rtt109 or which residues it preferentially acetylates. In the present study, we utilized a label-free quantitative mass spectrometry-based method to determine the steady-state kinetic parameters of acetylation catalyzed by Rtt109-Vps75 on H3 monomer, H3/H4 tetramer, and H3/H4-Asf1 complex. These results show that among these histone conformations, only H3K9 and H3K23 are significantly acetylated under steady-state conditions and that Asf1 promotes H3/H4 acetylation by Rtt109-Vps75. Asf1 equally increases the Rtt109-Vps75 specificity for both of these residues with a maximum stoichiometry of 1:1 (Asf1 to H3/H4), but does not alter the selectivity between these two residues. These data suggest that the H3/H4-Asf1 complex is a substrate for Rtt109-Vps75 without altering selectivity between residues. The deletion of either Rtt109 or Asf1 in vivo results in the same reduction of H3K9 acetylation, suggesting that Asf1 is required for efficient H3K9 acetylation both in vitro and in vivo. Furthermore, we found that the acetylation preference...Continue Reading

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Citations

Sep 1, 2015·Biochimica Et Biophysica Acta·Yin-Ming KuoAndrew J Andrews
Jan 5, 2018·Nucleic Acids Research·Lukas LercherTeresa Carlomagno
Aug 8, 2019·Nature Communications·Nataliya DanilenkoTeresa Carlomagno
Oct 1, 2015·The Biochemical Journal·Yin-Ming KuoAndrew J Andrews
Jun 14, 2019·Nucleic Acids Research·Joy M CoteAndrew J Andrews
Jun 5, 2021·DNA Repair·Ian Hammond-MartelHugo Wurtele

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Methods Mentioned

BETA
acetylation
histone acetylation
primary
acetylating

Software Mentioned

Xcalibur

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