Ethical Approval: No part of the contents of this chapter requires ethical review.
Informed Consent: No part of the contents of this chapter requires informed consent.
References
1. Taunton J, Hassig CA, Schreiber SL (1996) A mammalian histone deacetylase related to the
yeast transcriptional regulator Rpd3p. Science 272(5260):408–410
2. Verdin E, Ott M (2015) 50 years of protein acetylation: from gene regulation to epigenetics,
metabolism and beyond. Nat Rev Mol Cell Biol 16(4):258–264
3. Allfrey V, Faulkner R, Mirsky A (1964) Acetylation and methylation of histones and their
possible role in the regulation of RNA synthesis. PNAS 51(5):786–794
4. Gregoretti IV, Lee Y-M, Goodson HV (2004) Molecular evolution of the histone deacetylase
family: functional implications of phylogenetic analysis. J Mol Biol 338(1):17–31
5. Frye RA (2000) Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins.
Biochem Biophys Res Commun 273(2):793–798
6. Yang X-J, Seto E (2008) The Rpd3/Hda1 family of lysine deacetylases: from bacteria and
yeast to mice and men. Nat Rev Mol Cell Biol 9(3):206–218
7. Arrowsmith CH, Bountra C, Fish PV, Lee K, Schapira M (2012) Epigenetic protein families:
a new frontier for drug discovery. Nat Rev Drug Discov 11(5):384–400
8. Millard CJ, Watson PJ, Fairall L, Schwabe JWR (2017) Targeting class I histone deacetylases in
a “complex” environment. Trends Pharmacol Sci 38(4):363–377
9. Falkenberg KJ, Johnstone RW (2014) Histone deacetylases and their inhibitors in cancer,
neurological diseases and immune disorders. Nat Rev Drug Discov 13(9):673–691
10. Chakrabarti A, Oehme I, Witt O, Oliveira G, Sippl W, Romier C, Pierce RJ, Jung M (2015)
HDAC8: a multifaceted target for therapeutic interventions. Trends Pharmacol Sci 36(7):
481–492
11. Wei W, Liu X, Chen J, Gao S, Lu L, Zhang H, Ding G, Wang Z, Chen Z, Shi T, Li J, Yu J,
Wong J (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
12. Fellows R, Denizot J, Stellato C, Cuomo A, Jain P, Stoyanova E, Balázsi S, Hajnády Z,
Liebert A, Kazakevych J, Blackburn H, Correa RO, Fachi JL, Sato FT, Ribeiro WR, Ferreira
CM, Peree H, Spagnuolo M, Mattiuz R, Matolcsi C, Guedes J, Clark J, Veldhoen M, Bonaldi T,
Ramirez Vinolo MA, Varga-Weisz P (2018) Microbiota derived short chain fatty acids promote
histone crotonylation in the colon through histone deacetylases. Nat Commun 9(105):1–15
13. Bradner JE, West N, Grachan ML, Greenberg EF, Haggarty SJ, Warnow T, Mazitschek R
(2010) Chemical phylogenetics of histone deacetylases. Nat Chem Biol 6(3):238–243
14. Lahm A, Paolini C, Pallaoro M, Nardi M, Jones P, Neddermann P, Sambucini S, Bottomley M,
Surdo PL, Carfı A, Koch U, De Francesco R, Seinkühler C, Gallinari P (2007) Unraveling
the hidden catalytic activity of vertebrate class IIa histone deacetylases. PNAS 104(44):
17335–17340
15. Kutil Z, Novakova Z, Meleshin M, Mikesova J, Schutkowski M, Barinka C (2018)
Histone deacetylase 11 is a fatty-acid deacylase. ACS Chem Biol 13(3):685–693
16. Cao J, Sun L, Aramsangtienchai P, Spiegelman NA, Zhang X, Seto E, Lin H (2019) HDAC11
regulates type I interferon signaling through defatty-acylation of Shmt2. PNAS 116(12):
5487–5492
17. Moreno-Yruela C, Galleano I, Madsen AS, Olsen CA (2018) Histone deacetylase 11 is an Ε-Nmyristoyllysine hydrolase. Cell Chem Biol 25(7):849–856
18. Hai Y, Shinsky SA, Porter NJ, Christianson DW (2017) Histone deacetylase 10 structure and
molecular function as a polyamine deacetylase. Nat Commun 8(15368):1–9
19. Riggs MG, Whittaker RG, Neumann JR, Ingram VM (1977) N-butyrate causes histone modification in HeLa and Friend erythroleukaemia cells. Nature 268(5619):462–464
Hydroxamic Acid-Containing Peptides in the Study of Histone Deacetylases
49
Informed Consent: No part of the contents of this chapter requires informed consent.
References
1. Taunton J, Hassig CA, Schreiber SL (1996) A mammalian histone deacetylase related to the
yeast transcriptional regulator Rpd3p. Science 272(5260):408–410
2. Verdin E, Ott M (2015) 50 years of protein acetylation: from gene regulation to epigenetics,
metabolism and beyond. Nat Rev Mol Cell Biol 16(4):258–264
3. Allfrey V, Faulkner R, Mirsky A (1964) Acetylation and methylation of histones and their
possible role in the regulation of RNA synthesis. PNAS 51(5):786–794
4. Gregoretti IV, Lee Y-M, Goodson HV (2004) Molecular evolution of the histone deacetylase
family: functional implications of phylogenetic analysis. J Mol Biol 338(1):17–31
5. Frye RA (2000) Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins.
Biochem Biophys Res Commun 273(2):793–798
6. Yang X-J, Seto E (2008) The Rpd3/Hda1 family of lysine deacetylases: from bacteria and
yeast to mice and men. Nat Rev Mol Cell Biol 9(3):206–218
7. Arrowsmith CH, Bountra C, Fish PV, Lee K, Schapira M (2012) Epigenetic protein families:
a new frontier for drug discovery. Nat Rev Drug Discov 11(5):384–400
8. Millard CJ, Watson PJ, Fairall L, Schwabe JWR (2017) Targeting class I histone deacetylases in
a “complex” environment. Trends Pharmacol Sci 38(4):363–377
9. Falkenberg KJ, Johnstone RW (2014) Histone deacetylases and their inhibitors in cancer,
neurological diseases and immune disorders. Nat Rev Drug Discov 13(9):673–691
10. Chakrabarti A, Oehme I, Witt O, Oliveira G, Sippl W, Romier C, Pierce RJ, Jung M (2015)
HDAC8: a multifaceted target for therapeutic interventions. Trends Pharmacol Sci 36(7):
481–492
11. Wei W, Liu X, Chen J, Gao S, Lu L, Zhang H, Ding G, Wang Z, Chen Z, Shi T, Li J, Yu J,
Wong J (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
12. Fellows R, Denizot J, Stellato C, Cuomo A, Jain P, Stoyanova E, Balázsi S, Hajnády Z,
Liebert A, Kazakevych J, Blackburn H, Correa RO, Fachi JL, Sato FT, Ribeiro WR, Ferreira
CM, Peree H, Spagnuolo M, Mattiuz R, Matolcsi C, Guedes J, Clark J, Veldhoen M, Bonaldi T,
Ramirez Vinolo MA, Varga-Weisz P (2018) Microbiota derived short chain fatty acids promote
histone crotonylation in the colon through histone deacetylases. Nat Commun 9(105):1–15
13. Bradner JE, West N, Grachan ML, Greenberg EF, Haggarty SJ, Warnow T, Mazitschek R
(2010) Chemical phylogenetics of histone deacetylases. Nat Chem Biol 6(3):238–243
14. Lahm A, Paolini C, Pallaoro M, Nardi M, Jones P, Neddermann P, Sambucini S, Bottomley M,
Surdo PL, Carfı A, Koch U, De Francesco R, Seinkühler C, Gallinari P (2007) Unraveling
the hidden catalytic activity of vertebrate class IIa histone deacetylases. PNAS 104(44):
17335–17340
15. Kutil Z, Novakova Z, Meleshin M, Mikesova J, Schutkowski M, Barinka C (2018)
Histone deacetylase 11 is a fatty-acid deacylase. ACS Chem Biol 13(3):685–693
16. Cao J, Sun L, Aramsangtienchai P, Spiegelman NA, Zhang X, Seto E, Lin H (2019) HDAC11
regulates type I interferon signaling through defatty-acylation of Shmt2. PNAS 116(12):
5487–5492
17. Moreno-Yruela C, Galleano I, Madsen AS, Olsen CA (2018) Histone deacetylase 11 is an Ε-Nmyristoyllysine hydrolase. Cell Chem Biol 25(7):849–856
18. Hai Y, Shinsky SA, Porter NJ, Christianson DW (2017) Histone deacetylase 10 structure and
molecular function as a polyamine deacetylase. Nat Commun 8(15368):1–9
19. Riggs MG, Whittaker RG, Neumann JR, Ingram VM (1977) N-butyrate causes histone modification in HeLa and Friend erythroleukaemia cells. Nature 268(5619):462–464
Hydroxamic Acid-Containing Peptides in the Study of Histone Deacetylases
49