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Volumn 391, Issue 5, 2009, Pages 833-848

Histone Deacetylases Regulate Multicellular Development in the Social Amoeba Dictyostelium discoideum

Author keywords

cell adhesion; cyclic AMP; heterochrony; histone acetylation; trichostatin A

Indexed keywords

CYCLIC AMP; HDAB PROTEIN; HISTONE DEACETYLASE; TRICHOSTATIN A; UNCLASSIFIED DRUG;

EID: 68349089153     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.06.067     Document Type: Article
Times cited : (11)

References (60)
  • 1
    • 0242287927 scopus 로고    scopus 로고
    • The eukaryotic genome: a system regulated at different hierarchical levels
    • van Driel R., Fransz P.F., and Verschure P.J. The eukaryotic genome: a system regulated at different hierarchical levels. J. Cell Sci. 116 (2003) 4067-4075
    • (2003) J. Cell Sci. , vol.116 , pp. 4067-4075
    • van Driel, R.1    Fransz, P.F.2    Verschure, P.J.3
  • 3
    • 14844360104 scopus 로고    scopus 로고
    • Regulated chromatin domain comprising cluster of co-expressed genes in Drosophila melanogaster
    • Kalmykova A.I., Nurminsky D.I., Ryzhov D.V., and Shevelyov Y.Y. Regulated chromatin domain comprising cluster of co-expressed genes in Drosophila melanogaster. Nucleic Acids Res. 33 (2005) 1435-1444
    • (2005) Nucleic Acids Res. , vol.33 , pp. 1435-1444
    • Kalmykova, A.I.1    Nurminsky, D.I.2    Ryzhov, D.V.3    Shevelyov, Y.Y.4
  • 4
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specific histone acetylation and deacetylation
    • Shahbazian M.D., and Grunstein M. Functions of site-specific histone acetylation and deacetylation. Annu. Re. Biochem. 76 (2007) 75-100
    • (2007) Annu. Re. Biochem. , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 5
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo M.H., and Allis C.D. Roles of histone acetyltransferases and deacetylases in gene regulation. BioEssays 20 (1998) 615-626
    • (1998) BioEssays , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 6
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
    • Yang X.J., and Seto E. The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. Nature Rev. Mol. Cell Biol. 9 (2008) 206-218
    • (2008) Nature Rev. Mol. Cell Biol. , vol.9 , pp. 206-218
    • Yang, X.J.1    Seto, E.2
  • 7
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis
    • Gregoretti I.V., Lee Y.M., and Goodson H.V. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J. Mol. Biol. 338 (2004) 17-31
    • (2004) J. Mol. Biol. , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 9
    • 55549094833 scopus 로고    scopus 로고
    • Structural and functional analysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain
    • Bottomley M.J., Lo Surdo P., Di Giovine P., Cirillo A., Scarpelli R., Ferrigno F., et al. Structural and functional analysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain. J. Biol. Chem. 283 (2008) 26694-26704
    • (2008) J. Biol. Chem. , vol.283 , pp. 26694-26704
    • Bottomley, M.J.1    Lo Surdo, P.2    Di Giovine, P.3    Cirillo, A.4    Scarpelli, R.5    Ferrigno, F.6
  • 10
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: implications for disease and therapy
    • Haberland M., Montgomery R.L., and Olson E.N. The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nature Rev. Genet. 10 (2009) 32-42
    • (2009) Nature Rev. Genet. , vol.10 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 11
    • 59649092334 scopus 로고    scopus 로고
    • Zn(II)-dependent histone deacetylase inhibitors: suberoylanilide hydroxamic acid and trichostatin A
    • Codd R., Braich N., Liu J., Soe C.Z., and Pakchung A.A. Zn(II)-dependent histone deacetylase inhibitors: suberoylanilide hydroxamic acid and trichostatin A. Int. J. Biochem. Cell Biol. 41 (2009) 736-739
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 736-739
    • Codd, R.1    Braich, N.2    Liu, J.3    Soe, C.Z.4    Pakchung, A.A.5
  • 12
    • 0022763987 scopus 로고
    • Regulation of histone acetylation during macronuclear differentiation in Tetrahymena: evidence for control at the level of acetylation and deacetylation
    • Chicoine L.G., and Allis C.D. Regulation of histone acetylation during macronuclear differentiation in Tetrahymena: evidence for control at the level of acetylation and deacetylation. Dev. Biol. 116 (1986) 477-485
    • (1986) Dev. Biol. , vol.116 , pp. 477-485
    • Chicoine, L.G.1    Allis, C.D.2
  • 13
    • 33749669082 scopus 로고    scopus 로고
    • Histone H2B deacetylation at lysine 11 is required for yeast apoptosis induced by phosphorylation of H2B at serine 10
    • Ahn S.H., Diaz R.L., Grunstein M., and Allis C.D. Histone H2B deacetylation at lysine 11 is required for yeast apoptosis induced by phosphorylation of H2B at serine 10. Mol. Cell 24 (2006) 211-220
    • (2006) Mol. Cell , vol.24 , pp. 211-220
    • Ahn, S.H.1    Diaz, R.L.2    Grunstein, M.3    Allis, C.D.4
  • 14
    • 48249157844 scopus 로고    scopus 로고
    • Histone deacetylase genes in Arabidopsis development
    • Hollender C., and Liu Z. Histone deacetylase genes in Arabidopsis development. J. Integr. Plant Biol. 50 (2008) 875-885
    • (2008) J. Integr. Plant Biol. , vol.50 , pp. 875-885
    • Hollender, C.1    Liu, Z.2
  • 15
    • 42649093467 scopus 로고    scopus 로고
    • Histone deacetylase 3 (hdac3) is specifically required for liver development in zebrafish
    • Farooq M., Sulochana K.N., Pan X., To J., Sheng D., Gong Z., and Ge R. Histone deacetylase 3 (hdac3) is specifically required for liver development in zebrafish. Dev. Biol. 317 (2008) 336-353
    • (2008) Dev. Biol. , vol.317 , pp. 336-353
    • Farooq, M.1    Sulochana, K.N.2    Pan, X.3    To, J.4    Sheng, D.5    Gong, Z.6    Ge, R.7
  • 16
    • 42049099275 scopus 로고    scopus 로고
    • Complementary roles for histone deacetylases 1, 2, and 3 in differentiation of pluripotent stem cells
    • Humphrey G.W., Wang Y.H., Hirai T., Padmanabhan R., Panchision D.M., Newell L.F., et al. Complementary roles for histone deacetylases 1, 2, and 3 in differentiation of pluripotent stem cells. Differentiation 76 (2008) 348-356
    • (2008) Differentiation , vol.76 , pp. 348-356
    • Humphrey, G.W.1    Wang, Y.H.2    Hirai, T.3    Padmanabhan, R.4    Panchision, D.M.5    Newell, L.F.6
  • 18
    • 0003836640 scopus 로고    scopus 로고
    • Dictyostelium: Evolution, Cell Biology, and the Development of Multicellularity
    • Bard J., Barlow P., and Kirk D. (Eds), Cambridge University Press, Cambridge, UK
    • Kessin R. Dictyostelium: Evolution, Cell Biology, and the Development of Multicellularity. In: Bard J., Barlow P., and Kirk D. (Eds). Developmental and Cell Biology series (2001), Cambridge University Press, Cambridge, UK
    • (2001) Developmental and Cell Biology series
    • Kessin, R.1
  • 19
    • 33745602760 scopus 로고    scopus 로고
    • Transcriptional regulation of Dictyostelium pattern formation
    • Williams J.G. Transcriptional regulation of Dictyostelium pattern formation. EMBO Rep. 7 (2006) 694-698
    • (2006) EMBO Rep. , vol.7 , pp. 694-698
    • Williams, J.G.1
  • 20
    • 0001294643 scopus 로고
    • Pseudoplasmodium formation and organisation in Dictyostelium discoideum
    • Raper K. Pseudoplasmodium formation and organisation in Dictyostelium discoideum. J. Elisha Mitchell Sci. Soc. 56 (1940) 241-282
    • (1940) J. Elisha Mitchell Sci. Soc. , vol.56 , pp. 241-282
    • Raper, K.1
  • 21
    • 23244432717 scopus 로고    scopus 로고
    • Developmental decisions in Dictyostelium discoideum
    • Strmecki L., Greene D.M., and Pears C.J. Developmental decisions in Dictyostelium discoideum. Dev. Biol. 284 (2005) 25-36
    • (2005) Dev. Biol. , vol.284 , pp. 25-36
    • Strmecki, L.1    Greene, D.M.2    Pears, C.J.3
  • 22
    • 0036336886 scopus 로고    scopus 로고
    • A transcriptional profile of multicellular development in Dictyostelium discoideum
    • van Driessche N., Shaw C., Katoh M., Morio T., Sucgang R., Ibarra M., et al. A transcriptional profile of multicellular development in Dictyostelium discoideum. Development 129 (2002) 1543-1552
    • (2002) Development , vol.129 , pp. 1543-1552
    • van Driessche, N.1    Shaw, C.2    Katoh, M.3    Morio, T.4    Sucgang, R.5    Ibarra, M.6
  • 25
    • 33646140512 scopus 로고    scopus 로고
    • Developmental timing in Dictyostelium is regulated by the Set1 histone methyltransferase
    • Chubb J.R., Bloomfield G., Xu Q., Kaller M., Ivens A., Skelton J., et al. Developmental timing in Dictyostelium is regulated by the Set1 histone methyltransferase. Dev. Biol. 292 (2006) 519-532
    • (2006) Dev. Biol. , vol.292 , pp. 519-532
    • Chubb, J.R.1    Bloomfield, G.2    Xu, Q.3    Kaller, M.4    Ivens, A.5    Skelton, J.6
  • 26
    • 0042232109 scopus 로고    scopus 로고
    • Genome-wide expression analyses of gene regulation during early development of Dictyostelium discoideum
    • Iranfar N., Fuller D., and Loomis W.F. Genome-wide expression analyses of gene regulation during early development of Dictyostelium discoideum. Eukaryot. Cell 2 (2003) 664-670
    • (2003) Eukaryot. Cell , vol.2 , pp. 664-670
    • Iranfar, N.1    Fuller, D.2    Loomis, W.F.3
  • 27
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • Finnin M.S., Donigian J.R., Cohen A., Richon V.M., Rifkind R.A., Marks P.A., et al. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401 (1999) 188-193
    • (1999) Nature , vol.401 , pp. 188-193
    • Finnin, M.S.1    Donigian, J.R.2    Cohen, A.3    Richon, V.M.4    Rifkind, R.A.5    Marks, P.A.6
  • 28
    • 6344222799 scopus 로고    scopus 로고
    • Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor
    • Vannini A., Volpari C., Filocamo G., Casavola E.C., Brunetti M., Renzoni D., et al. Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor. Proc. Natl Acad. Sci. USA 101 (2004) 15064-15069
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 15064-15069
    • Vannini, A.1    Volpari, C.2    Filocamo, G.3    Casavola, E.C.4    Brunetti, M.5    Renzoni, D.6
  • 29
    • 45549095066 scopus 로고    scopus 로고
    • Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity
    • Schuetz A., Min J., Allali-Hassani A., Schapira M., Shuen M., Loppnau P., et al. Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity. J. Biol. Chem. 283 (2008) 11355-11363
    • (2008) J. Biol. Chem. , vol.283 , pp. 11355-11363
    • Schuetz, A.1    Min, J.2    Allali-Hassani, A.3    Schapira, M.4    Shuen, M.5    Loppnau, P.6
  • 30
    • 0018502551 scopus 로고
    • Oscillations of cyclic nucleotide concentrations in relation to the excitability of Dictyostelium cells
    • Gerisch G., Malchow D., Roos W., and Wick U. Oscillations of cyclic nucleotide concentrations in relation to the excitability of Dictyostelium cells. J. Exp. Biol. 81 (1979) 33-47
    • (1979) J. Exp. Biol. , vol.81 , pp. 33-47
    • Gerisch, G.1    Malchow, D.2    Roos, W.3    Wick, U.4
  • 31
    • 0002003316 scopus 로고
    • Aspects of aggregation in cellular slime moulds. I. Orientation and chemotaxis
    • Shaffer B.M. Aspects of aggregation in cellular slime moulds. I. Orientation and chemotaxis. Am. Nat. 91 (1957) 19-35
    • (1957) Am. Nat. , vol.91 , pp. 19-35
    • Shaffer, B.M.1
  • 32
    • 9244228550 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion during Dictyostelium development
    • Siu C.H., Harris T.J., Wang J., and Wong E. Regulation of cell-cell adhesion during Dictyostelium development. Semin. Cell Dev. Biol. 15 (2004) 633-641
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 633-641
    • Siu, C.H.1    Harris, T.J.2    Wang, J.3    Wong, E.4
  • 33
    • 0005619799 scopus 로고
    • Quantitation of membrane sites in aggregating Dictyostelium cells by use of tritiated univalent antibody
    • Beug H., Katz F.E., Stein A., and Gerisch G. Quantitation of membrane sites in aggregating Dictyostelium cells by use of tritiated univalent antibody. Proc. Natl Acad. Sci. USA 70 (1973) 3150-3154
    • (1973) Proc. Natl Acad. Sci. USA , vol.70 , pp. 3150-3154
    • Beug, H.1    Katz, F.E.2    Stein, A.3    Gerisch, G.4
  • 34
  • 35
    • 58549103327 scopus 로고    scopus 로고
    • The origins of multicellularity and the early history of the genetic toolkit for animal development
    • Rokas A. The origins of multicellularity and the early history of the genetic toolkit for animal development. Annu. Rev. Genet. 42 (2008) 235-251
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 235-251
    • Rokas, A.1
  • 36
    • 0037138363 scopus 로고    scopus 로고
    • Bromodomain: an acetyl-lysine binding domain
    • Zeng L., and Zhou M.M. Bromodomain: an acetyl-lysine binding domain. FEBS Lett. 513 (2002) 124-128
    • (2002) FEBS Lett. , vol.513 , pp. 124-128
    • Zeng, L.1    Zhou, M.M.2
  • 37
    • 33846014703 scopus 로고    scopus 로고
    • An acetylation site in the middle domain of Hsp90 regulates chaperone function
    • Scroggins B.T., Robzyk K., Wang D., Marcu M.G., Tsutsumi S., Beebe K., et al. An acetylation site in the middle domain of Hsp90 regulates chaperone function. Mol. Cell 25 (2007) 151-159
    • (2007) Mol. Cell , vol.25 , pp. 151-159
    • Scroggins, B.T.1    Robzyk, K.2    Wang, D.3    Marcu, M.G.4    Tsutsumi, S.5    Beebe, K.6
  • 38
    • 0036261826 scopus 로고    scopus 로고
    • The diversity of acetylated proteins
    • Polevoda, B. & Sherman, F. (2002). The diversity of acetylated proteins. Genome Biol. 3, r0006.
    • (2002) Genome Biol , vol.3
    • Polevoda, B.1    Sherman, F.2
  • 41
    • 0004277686 scopus 로고
    • Princeton University Press, Princeton
    • Bonner J.T. Size and Cycle (1965), Princeton University Press, Princeton
    • (1965) Size and Cycle
    • Bonner, J.T.1
  • 45
    • 0023217077 scopus 로고
    • Biochemical and morphological effects of sodium butyrate on Dictyostelium discoideum development
    • Boto L., Cano A., and Pestana A. Biochemical and morphological effects of sodium butyrate on Dictyostelium discoideum development. Mol. Cell Biochem. 74 (1987) 137-147
    • (1987) Mol. Cell Biochem. , vol.74 , pp. 137-147
    • Boto, L.1    Cano, A.2    Pestana, A.3
  • 46
    • 34547746013 scopus 로고    scopus 로고
    • Trichostatin A effects on gene expression in the protozoan parasite Entamoeba histolytica
    • Ehrenkaufer G.M., Eichinger D.J., and Singh U. Trichostatin A effects on gene expression in the protozoan parasite Entamoeba histolytica. BMC Genomics 8 (2007) 216
    • (2007) BMC Genomics , vol.8 , pp. 216
    • Ehrenkaufer, G.M.1    Eichinger, D.J.2    Singh, U.3
  • 47
    • 0020645943 scopus 로고
    • Proportion regulation without pattern formation in Dictyostelium discoideum
    • Oyama M., Okamoto K., and Takeuchi I. Proportion regulation without pattern formation in Dictyostelium discoideum. J. Embryol. Exp. Morphol. 75 (1983) 293-301
    • (1983) J. Embryol. Exp. Morphol. , vol.75 , pp. 293-301
    • Oyama, M.1    Okamoto, K.2    Takeuchi, I.3
  • 48
    • 4544357380 scopus 로고    scopus 로고
    • A demonstration of pattern formation without positional information in Dictyostelium
    • Thompson C.R., Reichelt S., and Kay R.R. A demonstration of pattern formation without positional information in Dictyostelium. Dev. Growth Differ. 46 (2004) 363-369
    • (2004) Dev. Growth Differ. , vol.46 , pp. 363-369
    • Thompson, C.R.1    Reichelt, S.2    Kay, R.R.3
  • 49
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: molecular mechanisms of action
    • Xu W.S., Parmigiani R.B., and Marks P.A. Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene 26 (2007) 5541-5552
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 50
    • 34250326306 scopus 로고    scopus 로고
    • Butyrate mediates decrease of histone acetylation centered on transcription start sites and down-regulation of associated genes
    • Rada-Iglesias A., Enroth S., Ameur A., Koch C.M., Clelland G.K., Respuela-Alonso P., et al. Butyrate mediates decrease of histone acetylation centered on transcription start sites and down-regulation of associated genes. Genome Res. 17 (2007) 708-719
    • (2007) Genome Res. , vol.17 , pp. 708-719
    • Rada-Iglesias, A.1    Enroth, S.2    Ameur, A.3    Koch, C.M.4    Clelland, G.K.5    Respuela-Alonso, P.6
  • 51
    • 55949130909 scopus 로고    scopus 로고
    • cAMP oscillations during aggregation of Dictyostelium
    • Loomis W.F. cAMP oscillations during aggregation of Dictyostelium. Adv. Exp. Med. Biol. 641 (2008) 39-48
    • (2008) Adv. Exp. Med. Biol. , vol.641 , pp. 39-48
    • Loomis, W.F.1
  • 52
    • 0034255624 scopus 로고    scopus 로고
    • CBP1 associates with the Dictyostelium cytoskeleton and is important for normal cell aggregation under certain developmental conditions
    • Dharamsi A., Tessarolo D., Coukell B., and Pun J. CBP1 associates with the Dictyostelium cytoskeleton and is important for normal cell aggregation under certain developmental conditions. Exp. Cell Res. 258 (2000) 298-309
    • (2000) Exp. Cell Res. , vol.258 , pp. 298-309
    • Dharamsi, A.1    Tessarolo, D.2    Coukell, B.3    Pun, J.4
  • 53
    • 0020367767 scopus 로고
    • Evolutionary strategies and developmental constraints in the cellular slime molds
    • Bonner J.T. Evolutionary strategies and developmental constraints in the cellular slime molds. Am. Nat. 119 (1982) 530-552
    • (1982) Am. Nat. , vol.119 , pp. 530-552
    • Bonner, J.T.1
  • 54
    • 0035798406 scopus 로고    scopus 로고
    • Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure
    • Gough J., Karplus K., Hughey R., and Chothia C. Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure. J. Mol. Biol. 313 (2001) 903-919
    • (2001) J. Mol. Biol. , vol.313 , pp. 903-919
    • Gough, J.1    Karplus, K.2    Hughey, R.3    Chothia, C.4
  • 56
    • 0023073916 scopus 로고
    • Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions
    • Sussman M. Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions. Methods Cell Biol 28 (1987) 9-29
    • (1987) Methods Cell Biol , vol.28 , pp. 9-29
    • Sussman, M.1
  • 57
    • 34250765348 scopus 로고    scopus 로고
    • Transformation of Dictyostelium discoideum with plasmid DNA
    • Gaudet P., Pilcher K.E., Fey P., and Chisholm R.L. Transformation of Dictyostelium discoideum with plasmid DNA. Nat Protoc 2 (2007) 1317-13124
    • (2007) Nat Protoc , vol.2 , pp. 1317-13124
    • Gaudet, P.1    Pilcher, K.E.2    Fey, P.3    Chisholm, R.L.4
  • 58
    • 33845535627 scopus 로고    scopus 로고
    • Trishanku, a novel regulator of cell-type stability and morphogenesis in Dictyostelium discoideum
    • Jaiswal J.K., Mujumdar N., Macwilliams H.K., and Nanjundiah V. Trishanku, a novel regulator of cell-type stability and morphogenesis in Dictyostelium discoideum. Differentiation 74 (2006) 596-607
    • (2006) Differentiation , vol.74 , pp. 596-607
    • Jaiswal, J.K.1    Mujumdar, N.2    Macwilliams, H.K.3    Nanjundiah, V.4
  • 60
    • 33750128476 scopus 로고    scopus 로고
    • Generation of multiple knockout mutants using the Cre-loxP system
    • Kimmel A.R., and Faix J. Generation of multiple knockout mutants using the Cre-loxP system. Methods Mol. Biol. 346 (2006) 187-199
    • (2006) Methods Mol. Biol. , vol.346 , pp. 187-199
    • Kimmel, A.R.1    Faix, J.2


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