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Volumn 15, Issue 8, 2003, Pages 1904-1917

Regulation and processing of maize histone deacetylase Hda1 by limited proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

GENES; MOLECULAR WEIGHT; MONOMERS; PROTEINS;

EID: 0041419235     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.013995     Document Type: Article
Times cited : (19)

References (51)
  • 1
    • 0034885934 scopus 로고    scopus 로고
    • Class II histone deacetylases: Structure, functions, and regulations
    • Bertos, N.R., Wang, A.M., and Yang, Y.J. (2001). Class II histone deacetylases: Structure, functions, and regulations. Biochem. Cell Biol. 79, 243-252.
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 243-252
    • Bertos, N.R.1    Wang, A.M.2    Yang, Y.J.3
  • 2
    • 0039776006 scopus 로고    scopus 로고
    • Technical advances: Transcriptional activator TGV mediates dexamethasone-inducible and tetracycline-inactivable gene expression
    • Bohner, S., Lenk, I.I., Rieping, M., Herold, M., and Gatz, C. (1999). Technical advances: Transcriptional activator TGV mediates dexamethasone-inducible and tetracycline-inactivable gene expression. Plant J. 19, 87-95.
    • (1999) Plant J. , vol.19 , pp. 87-95
    • Bohner, S.1    Lenk, I.I.2    Rieping, M.3    Herold, M.4    Gatz, C.5
  • 3
    • 0034653625 scopus 로고    scopus 로고
    • Identification of in-gel digested proteins by complementary peptide mass fingerprinting and tandem mass spectrometry data obtained on an electrospray ionization quadrupole time-of-flight mass spectrometer
    • Borchers, C., Peter, J.F., Hall, M.C., Kunkel, T.A., and Tomer, K.B. (2000). Identification of in-gel digested proteins by complementary peptide mass fingerprinting and tandem mass spectrometry data obtained on an electrospray ionization quadrupole time-of-flight mass spectrometer. Anal. Chem. 72, 1163-1168.
    • (2000) Anal. Chem. , vol.72 , pp. 1163-1168
    • Borchers, C.1    Peter, J.F.2    Hall, M.C.3    Kunkel, T.A.4    Tomer, K.B.5
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0026733493 scopus 로고
    • Specificity of Zea mays histone deacetylase is regulated by phosphorylation
    • Brosch, G., Georgieva, E., López-Rodas, G., Lindner, H., and Loidl, P. (1992). Specificity of Zea mays histone deacetylase is regulated by phosphorylation. J. Biol. Chem. 267, 20561-20564.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20561-20564
    • Brosch, G.1    Georgieva, E.2    López-Rodas, G.3    Lindner, H.4    Loidl, P.5
  • 7
    • 0030590475 scopus 로고    scopus 로고
    • Purification of histone deacetylase HD1-A of germinating maize embryos
    • Brosch, G., Goralik-Schramel, M., and Loidl, P. (1996). Purification of histone deacetylase HD1-A of germinating maize embryos. FEBS Lett. 393, 287-296.
    • (1996) FEBS Lett. , vol.393 , pp. 287-296
    • Brosch, G.1    Goralik-Schramel, M.2    Loidl, P.3
  • 8
    • 0029991514 scopus 로고    scopus 로고
    • HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex
    • Carmen, A.A., Rundlett, S.E., and Grunstein, M. (1996). HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex. J. Biol. Chem. 272, 15837-15844.
    • (1996) J. Biol. Chem. , vol.272 , pp. 15837-15844
    • Carmen, A.A.1    Rundlett, S.E.2    Grunstein, M.3
  • 9
    • 0034938473 scopus 로고    scopus 로고
    • Comparative analysis of HD2 type histone deacetylases in higher plants
    • Dangl, M., Brosch, G., Haas, H., Loidl, P., and Lusser, A. (2001). Comparative analysis of HD2 type histone deacetylases in higher plants. Planta 213, 280-285.
    • (2001) Planta , vol.213 , pp. 280-285
    • Dangl, M.1    Brosch, G.2    Haas, H.3    Loidl, P.4    Lusser, A.5
  • 10
    • 0034968451 scopus 로고    scopus 로고
    • Emerging connections between DNA methylation and histone acetylation
    • Dobosy, J.R., and Selker, E.U. (2001). Emerging connections between DNA methylation and histone acetylation. Cell. Mol. Life Sci. 58, 721-727.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 721-727
    • Dobosy, J.R.1    Selker, E.U.2
  • 11
    • 0033555764 scopus 로고    scopus 로고
    • Tetracycline-inducible expression systems with reduced basal activity in mammalian cells
    • Forster, K., Helbl, V., Lederer, T., Urlinger, S., Wittemburg, N., and Hillen, W. (1999). Tetracycline-inducible expression systems with reduced basal activity in mammalian cells. Nucleic Acids Res. 27, 708-710.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 708-710
    • Forster, K.1    Helbl, V.2    Lederer, T.3    Urlinger, S.4    Wittemburg, N.5    Hillen, W.6
  • 12
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single specific oligonucleotide primer
    • Frohman, M.A., Dush, M.K., and Martin, G.R. (1988). Rapid production of full-length cDNAs from rare transcripts: Amplification using a single specific oligonucleotide primer. Proc. Natl. Acad. Sci. USA 85, 8998-9002.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 14
    • 0034978613 scopus 로고    scopus 로고
    • Histone acetylation: Plants and fungi as model systems for the investigation of histone deacetylases
    • Graessle, S., Loidl, P., and Brosch, G. (2001). Histone acetylation: Plants and fungi as model systems for the investigation of histone deacetylases. Cell. Mol. Life Sci. 58, 704-720.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 704-720
    • Graessle, S.1    Loidl, P.2    Brosch, G.3
  • 16
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S., Armstrong, C.M., Kaeberlein, M., and Guarente, L. (2000). Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403, 795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 17
    • 0037324739 scopus 로고    scopus 로고
    • Structure and expression of the rice class-I type histone deacetylase genes OsHDAC1-3: OsHDAC1 overexpression in transgenic plants leads to increased growth rate and altered architecture
    • Jang, I.C., Pahk, Y.M., Song, S.I., Kwon, H.J., Nahm, B.H., and Kim, J.K. (2003). Structure and expression of the rice class-I type histone deacetylase genes OsHDAC1-3: OsHDAC1 overexpression in transgenic plants leads to increased growth rate and altered architecture. Plant J. 33, 531-541.
    • (2003) Plant J. , vol.33 , pp. 531-541
    • Jang, I.C.1    Pahk, Y.M.2    Song, S.I.3    Kwon, H.J.4    Nahm, B.H.5    Kim, J.K.6
  • 18
    • 0036181085 scopus 로고    scopus 로고
    • Pepsinogens, progastricsins, and prochymosins: Structure, function, evolution, and development
    • Kageyama, T. (2002). Pepsinogens, progastricsins, and prochymosins: Structure, function, evolution, and development. Cell. Mol. Life Sci. 59, 288-306.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 288-306
    • Kageyama, T.1
  • 20
    • 0033602995 scopus 로고    scopus 로고
    • Different types of maize histone deacetylases are distinguished by a highly complex substrate and site specificity
    • Kölle, D., Brosch, G., Lechner, T., Pipal, A., Helliger, W., Taplick, J., and Loidl, P. (1999). Different types of maize histone deacetylases are distinguished by a highly complex substrate and site specificity. Biochemistry 38, 6769-6773.
    • (1999) Biochemistry , vol.38 , pp. 6769-6773
    • Kölle, D.1    Brosch, G.2    Lechner, T.3    Pipal, A.4    Helliger, W.5    Taplick, J.6    Loidl, P.7
  • 23
    • 0023869751 scopus 로고
    • Towards an understanding of the biological function of histone acetylation
    • Loidl, P. (1988). Towards an understanding of the biological function of histone acetylation. FEBS Lett. 227, 91-95.
    • (1988) FEBS Lett. , vol.227 , pp. 91-95
    • Loidl, P.1
  • 24
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • Luo, J., Nikolaev, A.Y., Imai, S., Chen, D., Su, F., Shiloh, A., Guarente, L., and Gu, W. (2001). Negative control of p53 by Sir2α promotes cell survival under stress. Cell 107, 137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 25
    • 0036779319 scopus 로고    scopus 로고
    • Acetylated, methylated, remodeled: Chromatin states for gene regulation
    • Lusser, A. (2002). Acetylated, methylated, remodeled: Chromatin states for gene regulation. Curr. Opin. Plant Biol. 5, 437-443.
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 437-443
    • Lusser, A.1
  • 26
    • 0030771898 scopus 로고    scopus 로고
    • Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein
    • Lusser, A., Brosch, G., Loidl, A., Haas, H., and Loidl, P. (1997). Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein. Science 277, 88-91.
    • (1997) Science , vol.277 , pp. 88-91
    • Lusser, A.1    Brosch, G.2    Loidl, A.3    Haas, H.4    Loidl, P.5
  • 27
    • 0035212791 scopus 로고    scopus 로고
    • Histone acetylation: Lessons from the plant kingdom
    • Lusser, A., Kölle, D., and Loidl, P. (2001). Histone acetylation: Lessons from the plant kingdom. Trends Plant Sci. 6, 59-65.
    • (2001) Trends Plant Sci. , vol.6 , pp. 59-65
    • Lusser, A.1    Kölle, D.2    Loidl, P.3
  • 28
    • 0035868764 scopus 로고    scopus 로고
    • Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription
    • Muth, V., Nadaud, S., Grummt, I., and Voit, R. (2001). Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription. EMBO J. 20, 1353-1362.
    • (2001) EMBO J. , vol.20 , pp. 1353-1362
    • Muth, V.1    Nadaud, S.2    Grummt, I.3    Voit, R.4
  • 29
    • 0033598804 scopus 로고    scopus 로고
    • PICKLE is a CHD3 chromatin-remodeling factor that regulates the transition from embryonic to vegetative development in Arabidopsis
    • Ogas, J., Kaufmann, S., Henderson, J., and Sommerville, C. (1999). PICKLE is a CHD3 chromatin-remodeling factor that regulates the transition from embryonic to vegetative development in Arabidopsis. Proc. Natl. Acad. Sci. USA 96, 13839-13844.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13839-13844
    • Ogas, J.1    Kaufmann, S.2    Henderson, J.3    Sommerville, C.4
  • 30
    • 0036929765 scopus 로고    scopus 로고
    • Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes
    • Pandey, R., Müller, A., Napoli, C.A., Slinger, D.A., Pikaard, C.S., Richards, E.J., Bender, J., Mount, D.W., and Jorgensen, R.A. (2002). Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes. Nucleic Acids Res. 30, 5036-5055.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5036-5055
    • Pandey, R.1    Müller, A.2    Napoli, C.A.3    Slinger, D.A.4    Pikaard, C.S.5    Richards, E.J.6    Bender, J.7    Mount, D.W.8    Jorgensen, R.A.9
  • 31
    • 0035861594 scopus 로고    scopus 로고
    • Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation
    • Pflum, M.K., Tong, U.K., Lane, W.S., and Schreiber, S.L. (2001). Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation. J. Biol. Chem. 276, 47733-47741.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47733-47741
    • Pflum, M.K.1    Tong, U.K.2    Lane, W.S.3    Schreiber, S.L.4
  • 32
    • 0032696747 scopus 로고    scopus 로고
    • Nucleolar dominance and silencing of transcription
    • Pikaard, C.S. (1999). Nucleolar dominance and silencing of transcription. Trends Plant Sci. 4, 478-483.
    • (1999) Trends Plant Sci. , vol.4 , pp. 478-483
    • Pikaard, C.S.1
  • 33
    • 0036851203 scopus 로고    scopus 로고
    • Chromatin-remodeling and memory factors: New regulators of plant development
    • Reyes, J.C., Hennig, L., and Gruissem, W. (2002). Chromatin-remodeling and memory factors: New regulators of plant development. Plant Physiol. 130, 1090-1101.
    • (2002) Plant Physiol. , vol.130 , pp. 1090-1101
    • Reyes, J.C.1    Hennig, L.2    Gruissem, W.3
  • 34
    • 0031865919 scopus 로고    scopus 로고
    • Identification and characterization of an RPD3 homologue from maize (Zea mays L.) that is able to complement an rpd3 null mutant of Saccharomyces cerevisiae
    • Rossi, V., Hartings, H., and Motto, M. (1998). Identification and characterization of an RPD3 homologue from maize (Zea mays L.) that is able to complement an rpd3 null mutant of Saccharomyces cerevisiae. Mol. Gen. Genet. 258, 288-296.
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 288-296
    • Rossi, V.1    Hartings, H.2    Motto, M.3
  • 36
    • 0029856225 scopus 로고    scopus 로고
    • HDA1 and RPD3 are members of distinct histone deacetylase complexes that regulate silencing and transcription
    • Rundlett, S.E., Carmen, A.A., Kobayashi, R., Bavykin, S., Turner, B.M., and Grunstein, M. (1996). HDA1 and RPD3 are members of distinct histone deacetylase complexes that regulate silencing and transcription. Proc. Natl. Acad. Sci. USA 93, 14503-14508.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14503-14508
    • Rundlett, S.E.1    Carmen, A.A.2    Kobayashi, R.3    Bavykin, S.4    Turner, B.M.5    Grunstein, M.6
  • 37
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRTS is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • Schwer, B., North, B.J., Frye, R.A., Ott, M., and Verdin, E. (2002). The human silent information regulator (Sir)2 homologue hSIRTS is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J. Cell Biol. 158, 647-657.
    • (2002) J. Cell Biol. , vol.158 , pp. 647-657
    • Schwer, B.1    North, B.J.2    Frye, R.A.3    Ott, M.4    Verdin, E.5
  • 38
    • 0343307146 scopus 로고    scopus 로고
    • Eukaryotic protein processing: Endoproteolysis of precursor proteins
    • Seidah, N.G., and Chrétien, M. (1997). Eukaryotic protein processing: Endoproteolysis of precursor proteins. Curr. Opin. Biotechnol. 8, 602-607.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 602-607
    • Seidah, N.G.1    Chrétien, M.2
  • 39
    • 0020629532 scopus 로고
    • Two adjacent genomic zein sequences: Structure, organization and tissue-specific restriction pattern
    • Spena, A., Viotti, A., and Pirrotta, V. (1983). Two adjacent genomic zein sequences: Structure, organization and tissue-specific restriction pattern. J. Mol. Biol. 169, 799-811.
    • (1983) J. Mol. Biol. , vol.169 , pp. 799-811
    • Spena, A.1    Viotti, A.2    Pirrotta, V.3
  • 40
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B.D., and Allis, C.D. (2000). The language of covalent histone modifications. Nature 403, 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 41
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3
    • Taunton, J., Hassig, C.A., and Schreiber, S.L. (1996). A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3. Science 272, 408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 42
    • 0035793060 scopus 로고    scopus 로고
    • Blocking histone deacetylation in Arabidopsis induces pleiotropic effects on plant gene regulation and development
    • Tian, L., and Chen, Z.J. (2001). Blocking histone deacetylation in Arabidopsis induces pleiotropic effects on plant gene regulation and development. Proc. Natl. Acad. Sci. USA 98, 200-205.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 200-205
    • Tian, L.1    Chen, Z.J.2
  • 43
    • 0024024137 scopus 로고
    • Functional dissection of VP16, the transactivator of herpes simplex virus immediate early gene expression
    • Triezenberg, S.J., Kingsbury, R.C., and McKnight, S.L. (1988). Functional dissection of VP16, the transactivator of herpes simplex virus immediate early gene expression. Genes Dev. 2, 718-729.
    • (1988) Genes Dev. , vol.2 , pp. 718-729
    • Triezenberg, S.J.1    Kingsbury, R.C.2    McKnight, S.L.3
  • 44
    • 0037199944 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 2 by protein kinase CK2
    • Tsai, S.C., and Seto, E. (2002). Regulation of histone deacetylase 2 by protein kinase CK2. J. Biol. Chem. 277, 31826-31833.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31826-31833
    • Tsai, S.C.1    Seto, E.2
  • 45
    • 0027525056 scopus 로고
    • Decoding the nucleosome
    • Turner, B.M. (1993). Decoding the nucleosome. Cell 8, 5-8.
    • (1993) Cell , vol.8 , pp. 5-8
    • Turner, B.M.1
  • 46
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T., and Mann, M. (1996). Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379, 466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 47
    • 0033675659 scopus 로고    scopus 로고
    • Functional analysis of a RPD3 histone deacetylase homolog in Arabidopsis thaliana
    • Wu, K., Malik, K., Tian, L., Brown, D., and Miki, B. (2000a). Functional analysis of a RPD3 histone deacetylase homolog in Arabidopsis thaliana. Plant Mol. Biol. 44, 167-176.
    • (2000) Plant Mol. Biol. , vol.44 , pp. 167-176
    • Wu, K.1    Malik, K.2    Tian, L.3    Brown, D.4    Miki, B.5
  • 48
    • 0034057586 scopus 로고    scopus 로고
    • Functional analysis of HD2 histone deacetylase homologues in Arabidopsis thaliana
    • Wu, K., Tian, L., Malik, K., Brown, D., and Miki, B. (2000b). Functional analysis of HD2 histone deacetylase homologues in Arabidopsis thaliana. Plant J. 22, 19-27.
    • (2000) Plant J. , vol.22 , pp. 19-27
    • Wu, K.1    Tian, L.2    Malik, K.3    Brown, D.4    Miki, B.5
  • 49
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida, M., Kijima, M., Akita, M., and Beppu, T. (1990). Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem. 265, 17174-17179.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 50
    • 0037162697 scopus 로고    scopus 로고
    • Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy
    • Zhang, C.L., McKinsey, T.A., Chang, S., Antos, C.L., Hill, J.A., and Olson, E.N. (2002). Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy. Cell 110, 479-488.
    • (2002) Cell , vol.110 , pp. 479-488
    • Zhang, C.L.1    McKinsey, T.A.2    Chang, S.3    Antos, C.L.4    Hill, J.A.5    Olson, E.N.6
  • 51
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S., and Matthias, P. (2003). HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J. 22, 1168-1179.
    • (2003) EMBO J. , vol.22 , pp. 1168-1179
    • Zhang, Y.1    Li, N.2    Caron, C.3    Matthias, G.4    Hess, D.5    Khochbin, S.6    Matthias, P.7


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