References
1. Allfrey VG, Faulkner R, Mirsky AE (1964)
Acetylation and methylation of histones and
their possible role in the regulation of rna synthesis. Proc Natl Acad Sci U S A 51:786–794
2. Riggs MG, Whittaker RG, Neumann JR,
Ingram VM (1977) n-Butyrate causes histone
modification in HeLa and friend erythroleukaemia cells. Nature 268:462. https://doi.
org/10.1038/268462a0
3. Taunton J, Hassig CA, Schreiber SL (1996) A
mammalian histone deacetylase related to the
yeast transcriptional regulator Rpd3p. Science
272:408
4. Yang WM, Inouye C, Zeng Y, Bearss D, Seto E
(1996) Transcriptional repression by YY1 is
mediated by interaction with a mammalian
homolog of the yeast global regulator RPD3.
Proc Natl Acad Sci U S A 93:12845–12850
5. Seto E, Yoshida M (2014) Erasers of histone
acetylation: the histone deacetylase enzymes.
Cold Spring Harb Perspect Biol 6:a018713.
https://doi.org/10.1101/cshperspect.
a018713
6. Sauve AA (2010) Sirtuin chemical mechanisms.
Biochim
Biophys
Acta
1804:1591–1603. https://doi.org/10.1016/
j.bbapap.2010.01.021
7. Lombardi PM, Cole KE, Dowling DP, Christianson DW (2011) Structure, mechanism, and
inhibition of histone deacetylases and related
metalloenzymes. Curr Opin Struct Biol
21:735–743. https://doi.org/10.1016/j.sbi.
2011.08.004
8. Tan M et al (2011) Identification of 67 histone
marks and histone lysine crotonylation as a new
type
of
histone
modification.
Cell
146:1016–1028. https://doi.org/10.1016/j.
cell.2011.08.008
9. Finkemeier I, Laxa M, Miguet L, Howden AJ,
Sweetlove LJ (2011) Proteins of diverse function and subcellular location are lysine acetylated
in
Arabidopsis.
Plant
Physiol
155:1779–1790. https://doi.org/10.1104/
pp.110.171595
10. Wu X et al (2011) Lysine acetylation is a widespread protein modification for diverse proteins
in Arabidopsis. Plant Physiol 155:1769–1778.
https://doi.org/10.1104/pp.110.165852
11. Henriksen P et al (2012) Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Mol
Cell Proteomics 11:1510–1522. https://doi.
org/10.1074/mcp.M112.017251
12. Colak G et al (2013) Identification of lysine
succinylation substrates and the succinylation
regulatory enzyme CobB in Escherichia coli.
Mol Cell Proteomics 12:3509–3520. https://
doi.org/10.1074/mcp.M113.031567
13. Vaziri H et al (2001) hSIR2(SIRT1) functions
as an NAD-dependent p53 deacetylase. Cell
107:149–159
14. Luo J, Su F, Chen D, Shiloh A, Gu W (2000)
Deacetylation of p53 modulates its effect on
cell
growth
and
apoptosis.
Nature
408:377–381.
https://doi.org/10.1038/
35042612
15. Hubbert C et al (2002) HDAC6 is a
microtubule-associated deacetylase. Nature
417:455–458.
https://doi.org/10.1038/
417455a
16. Andrews FH et al (2016) The Taf14 YEATS
domain is a reader of histone crotonylation.
Nat Chem Biol 12:396–398. https://doi.
org/10.1038/nchembio.2065
17. Sabari BR et al (2015) Intracellular crotonylCoA stimulates transcription through p300catalyzed histone crotonylation. Mol Cell
58:203–215.
https://doi.org/10.1016/j.
molcel.2015.02.029
18. Wei W et al (2017) Class I histone deacetylases
are major histone decrotonylases: evidence for
critical and broad function of histone crotonylation in transcription. Cell Res 27:898–915.
https://doi.org/10.1038/cr.2017.68
19. Meier K, Brehm A (2014) Chromatin regulation: how complex does it get? Epigenetics
9:1485–1495.
https://doi.org/10.4161/
15592294.2014.971580
20. Zhang Y, Iratni R, Erdjument-Bromage H,
Tempst P, Reinberg D (1997) Histone deacetylases and SAP18, a novel polypeptide, are
components of a human Sin3 complex. Cell
89:357–364.
https://doi.org/10.1016/
S0092-8674(00)80216-0
21. Xue Y et al (1998) NURD, a novel complex
with both ATP-dependent chromatin-remodeling and histone deacetylase activities. Mol
Cell 2:851–861
22. Wen YD et al (2000) The histone deacetylase-3
complex contains nuclear receptor corepressors. Proc Natl Acad Sci U S A 97:7202–7207
23. Simithy J et al (2017) Characterization of histone acylations links chromatin modifications
with metabolism. Nat Commun 8:1141.
https://doi.org/10.1038/s41467-01701384-9
24. Spinck M, Neumann-Staubitz P, Ecke M, Gasper R, Neumann H (2020) Evolved, selective
erasers of distinct lysine acylations. Angew
336
Martin Spinck et al.
1. Allfrey VG, Faulkner R, Mirsky AE (1964)
Acetylation and methylation of histones and
their possible role in the regulation of rna synthesis. Proc Natl Acad Sci U S A 51:786–794
2. Riggs MG, Whittaker RG, Neumann JR,
Ingram VM (1977) n-Butyrate causes histone
modification in HeLa and friend erythroleukaemia cells. Nature 268:462. https://doi.
org/10.1038/268462a0
3. Taunton J, Hassig CA, Schreiber SL (1996) A
mammalian histone deacetylase related to the
yeast transcriptional regulator Rpd3p. Science
272:408
4. Yang WM, Inouye C, Zeng Y, Bearss D, Seto E
(1996) Transcriptional repression by YY1 is
mediated by interaction with a mammalian
homolog of the yeast global regulator RPD3.
Proc Natl Acad Sci U S A 93:12845–12850
5. Seto E, Yoshida M (2014) Erasers of histone
acetylation: the histone deacetylase enzymes.
Cold Spring Harb Perspect Biol 6:a018713.
https://doi.org/10.1101/cshperspect.
a018713
6. Sauve AA (2010) Sirtuin chemical mechanisms.
Biochim
Biophys
Acta
1804:1591–1603. https://doi.org/10.1016/
j.bbapap.2010.01.021
7. Lombardi PM, Cole KE, Dowling DP, Christianson DW (2011) Structure, mechanism, and
inhibition of histone deacetylases and related
metalloenzymes. Curr Opin Struct Biol
21:735–743. https://doi.org/10.1016/j.sbi.
2011.08.004
8. Tan M et al (2011) Identification of 67 histone
marks and histone lysine crotonylation as a new
type
of
histone
modification.
Cell
146:1016–1028. https://doi.org/10.1016/j.
cell.2011.08.008
9. Finkemeier I, Laxa M, Miguet L, Howden AJ,
Sweetlove LJ (2011) Proteins of diverse function and subcellular location are lysine acetylated
in
Arabidopsis.
Plant
Physiol
155:1779–1790. https://doi.org/10.1104/
pp.110.171595
10. Wu X et al (2011) Lysine acetylation is a widespread protein modification for diverse proteins
in Arabidopsis. Plant Physiol 155:1769–1778.
https://doi.org/10.1104/pp.110.165852
11. Henriksen P et al (2012) Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Mol
Cell Proteomics 11:1510–1522. https://doi.
org/10.1074/mcp.M112.017251
12. Colak G et al (2013) Identification of lysine
succinylation substrates and the succinylation
regulatory enzyme CobB in Escherichia coli.
Mol Cell Proteomics 12:3509–3520. https://
doi.org/10.1074/mcp.M113.031567
13. Vaziri H et al (2001) hSIR2(SIRT1) functions
as an NAD-dependent p53 deacetylase. Cell
107:149–159
14. Luo J, Su F, Chen D, Shiloh A, Gu W (2000)
Deacetylation of p53 modulates its effect on
cell
growth
and
apoptosis.
Nature
408:377–381.
https://doi.org/10.1038/
35042612
15. Hubbert C et al (2002) HDAC6 is a
microtubule-associated deacetylase. Nature
417:455–458.
https://doi.org/10.1038/
417455a
16. Andrews FH et al (2016) The Taf14 YEATS
domain is a reader of histone crotonylation.
Nat Chem Biol 12:396–398. https://doi.
org/10.1038/nchembio.2065
17. Sabari BR et al (2015) Intracellular crotonylCoA stimulates transcription through p300catalyzed histone crotonylation. Mol Cell
58:203–215.
https://doi.org/10.1016/j.
molcel.2015.02.029
18. Wei W et al (2017) Class I histone deacetylases
are major histone decrotonylases: evidence for
critical and broad function of histone crotonylation in transcription. Cell Res 27:898–915.
https://doi.org/10.1038/cr.2017.68
19. Meier K, Brehm A (2014) Chromatin regulation: how complex does it get? Epigenetics
9:1485–1495.
https://doi.org/10.4161/
15592294.2014.971580
20. Zhang Y, Iratni R, Erdjument-Bromage H,
Tempst P, Reinberg D (1997) Histone deacetylases and SAP18, a novel polypeptide, are
components of a human Sin3 complex. Cell
89:357–364.
https://doi.org/10.1016/
S0092-8674(00)80216-0
21. Xue Y et al (1998) NURD, a novel complex
with both ATP-dependent chromatin-remodeling and histone deacetylase activities. Mol
Cell 2:851–861
22. Wen YD et al (2000) The histone deacetylase-3
complex contains nuclear receptor corepressors. Proc Natl Acad Sci U S A 97:7202–7207
23. Simithy J et al (2017) Characterization of histone acylations links chromatin modifications
with metabolism. Nat Commun 8:1141.
https://doi.org/10.1038/s41467-01701384-9
24. Spinck M, Neumann-Staubitz P, Ecke M, Gasper R, Neumann H (2020) Evolved, selective
erasers of distinct lysine acylations. Angew
336
Martin Spinck et al.